Table of Contents Author Guidelines Submit a Manuscript
BioMed Research International
Volume 2014, Article ID 273473, 24 pages
http://dx.doi.org/10.1155/2014/273473
Review Article

Autophagy in Drosophila: From Historical Studies to Current Knowledge

1School of Life Sciences, University of Warwick, Coventry CV4 7AL, UK
2Department of Anatomy, Cell and Developmental Biology, Eötvös Loránd University, Budapest H-1117, Hungary

Received 23 January 2014; Accepted 17 April 2014; Published 18 May 2014

Academic Editor: Rodney J. Devenish

Copyright © 2014 Nitha C. Mulakkal et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. S. Kaushik and A. M. Cuervo, “Chaperone-mediated autophagy: a unique way to enter the lysosome world,” Trends in Cell Biology, vol. 22, no. 8, pp. 407–417, 2012. View at Publisher · View at Google Scholar
  2. M. Locke and J. V. Collins, “The structure and formation of protein granules in the fat body of an insect,” The Journal of Cell Biology, vol. 26, no. 3, pp. 857–884, 1965. View at Publisher · View at Google Scholar
  3. D. Mijaljica, M. Prescott, and R. J. Devenish, “Microautophagy in mammalian cells: revisiting a 40-year-old conundrum,” Autophagy, vol. 7, no. 7, pp. 673–682, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. N. Mizushima and M. Komatsu, “Autophagy: renovation of cells and tissues,” Cell, vol. 147, no. 4, pp. 728–741, 2011. View at Publisher · View at Google Scholar · View at Scopus
  5. Z. Yang and D. J. Klionsky, “Eaten alive: a history of macroautophagy,” Nature Cell Biology, vol. 12, no. 9, pp. 814–822, 2010. View at Publisher · View at Google Scholar · View at Scopus
  6. A. B. Novikoff, “The proximal tubule cell in experimental hydronephrosis,” The Journal of Biophysical and Biochemical Cytology, vol. 6, no. 1, pp. 136–138, 1959. View at Publisher · View at Google Scholar
  7. A. B. Novikoff and E. Essner, “Cytolysomes and mitochondrial degeneration,” The Journal of Cell Biology, vol. 15, pp. 140–146, 1962. View at Google Scholar · View at Scopus
  8. T. P. Ashford and K. R. Porter, “Cytoplasmic components in hepatic cell lysosomes,” The Journal of Cell Biology, vol. 12, pp. 198–202, 1962. View at Google Scholar · View at Scopus
  9. R. L. Deter, P. Baudhuin, and C. De Duve, “Participation of lysosomes in cellular autophagy induced in rat liver by glucagon,” The Journal of Cell Biology, vol. 35, no. 2, pp. C11–C16, 1967. View at Google Scholar · View at Scopus
  10. U. Pfeifer, “Inhibition by insulin of the formation of autophagic vacuoles in rat liver. A morphometric approach to the kinetics of intracellular degradation by autophagy,” The Journal of Cell Biology, vol. 78, no. 1, pp. 152–167, 1978. View at Google Scholar · View at Scopus
  11. U. Pfeifer, “Inhibition by insulin of the physiological autophagic breakdown of cell organelles,” Acta Biologica et Medica Germanica, vol. 36, no. 11-12, pp. 1691–1694, 1977. View at Google Scholar · View at Scopus
  12. A. B. Novikoff, E. Essner, and N. Quintana, “Golgi apparatus and lysosomes,” Federation Proceedings, vol. 23, pp. 1010–1022, 1964. View at Google Scholar · View at Scopus
  13. A. V. S. de Reuck and M. P. Cameron, Ciba Foundation Symposium on Lysosomes, J.A. Churchill, London, UK, 1963.
  14. C. De Duve and R. Wattiaux, “Functions of lysosomes,” Annual Review of Physiology, vol. 28, pp. 435–492, 1966. View at Google Scholar · View at Scopus
  15. A. Berlese, “Osservazioni su fenomeni che avvengono durante la ninfosi insetti metabolici,” Rivista dì Patologia Vegetale, vol. 8, no. 1, 1899. View at Google Scholar
  16. G. H. Bishop, “Cell metabolism in the insect fat-body-I. Cytological changes accompanying growth and histolysis of the fat-body of Apis mellifica,” Journal of Morphology, vol. 36, pp. 567–601, 1922. View at Publisher · View at Google Scholar
  17. G. H. Bishop, “Cell metabolism in the insect fat-body-II. A functional interpretation of the changes in structure in the fat-body cells of the honey bee,” Journal of Morphology, vol. 37, pp. 533–553, 1923. View at Publisher · View at Google Scholar
  18. B. von Gaudecker, “Uber den Formwechsel einiger Zellorganelle bei der Bildung der Reservestoffe in Fettkorper von Drosophila-larven,” Zeitschrift für Zellforschung und Mikroskopische Anatomie, vol. 61, no. 1, pp. 56–95, 1963. View at Publisher · View at Google Scholar · View at Scopus
  19. M. Locke and J. V. Collins, “Protein uptake into multivesicular bodies and storage granules in the fat body of an insect,” The Journal of Cell Biology, vol. 36, no. 3, pp. 453–483, 1968. View at Google Scholar · View at Scopus
  20. F. M. Butterworth and E. C. Forrest, “Ultrastructure of the preparative phase of cell death in the larval fat body of Drosophila melanogaster,” Tissue and Cell, vol. 16, no. 2, pp. 237–250, 1984. View at Google Scholar · View at Scopus
  21. W. A. Thomasson and H. K. Mitchell, “Hormonal control of protein granule accumulation in fat bodies of Drosophila melanogaster larvae,” Journal of Insect Physiology, vol. 18, no. 10, pp. 1885–1899, 1972. View at Google Scholar · View at Scopus
  22. L. M. Riddiford, “Hormone receptors and the regulation of insect metamorphosis,” Receptor, vol. 3, no. 3, pp. 203–209, 1993. View at Google Scholar · View at Scopus
  23. J. V. Collins, “The hormonal control of fat body development in Calpodes ethlius (Lepidoptera, Hesperiidae),” Journal of Insect Physiology, vol. 15, no. 2, pp. 341–352, 1969. View at Google Scholar · View at Scopus
  24. M. Sass and J. Kovacs, “Ecdysterone and an analogue of juvenile hormone on the autophagy in the cells of fat body of Mamestra brassicae,” Acta Biologica Academiae Scientiarum Hungaricae, vol. 26, no. 3-4, pp. 189–196, 1975. View at Google Scholar · View at Scopus
  25. M. Sass and J. Kovacs, “The effect of ecdysone on the fat body cells of the penultimate larvae of Mamestra brassicae,” Cell and Tissue Research, vol. 180, no. 3, pp. 403–409, 1977. View at Google Scholar · View at Scopus
  26. V. B. Wigglesworth, “Cytological changes in the fat body of Rhodnius during starvation, feeding and oxygen want,” Journal of Cell Science, vol. 2, no. 2, pp. 243–256, 1967. View at Google Scholar · View at Scopus
  27. F. M. Butterworth, D. Bodenstein, and R. C. King, “Adipose tissue of Drosophila melanogaster. I. An experimental study of larval fat body,” The Journal of Experimental Zoology, vol. 158, pp. 141–153, 1965. View at Google Scholar · View at Scopus
  28. G. Beadle, E. L. Tatum, and C. W. Clancy, “Food level in relation to rate of development and eye pigmentation in Drosophila melanogaster,” The Biological Bulletin, vol. 75, pp. 447–462, 1938. View at Publisher · View at Google Scholar
  29. J. R. Shoup, “The development of pigment granules in the eyes of wild type and mutant Drosophila melanogaster,” The Journal of Cell Biology, vol. 29, no. 2, pp. 223–249, 1966. View at Google Scholar · View at Scopus
  30. R. A. Lockshin and C. M. Williams, “Programmed cell death-I. Cytology of degeneration in the intersegmental muscles of the Pernyi silkmoth,” Journal of Insect Physiology, vol. 11, no. 2, pp. 123–133, 1965. View at Google Scholar · View at Scopus
  31. R. A. Lockshin and C. M. Williams, “Programmed cell death-V. Cytolytic enzymes in relation to the breakdown of the intersegmental muscles of silkmoths,” Journal of Insect Physiology, vol. 11, no. 7, pp. 831–844, 1965. View at Google Scholar · View at Scopus
  32. J. Beaulaton and R. A. Lockshin, “Ultrastructural study of the normal degeneration of the intersegmental muscles of Antheraea polyphemus and Manduca sexta (Insecta, Lepidoptera) with particular reference to cellular autophagy,” Journal of Morphology, vol. 154, no. 1, pp. 39–57, 1977. View at Google Scholar · View at Scopus
  33. P. G. H. Clarke, “Developmental cell death: morphological diversity and multiple mechanisms,” Anatomy and Embryology, vol. 181, no. 3, pp. 195–213, 1990. View at Google Scholar · View at Scopus
  34. M. Tsukada and Y. Ohsumi, “Isolation and characterization of autophagy-defective mutants of Saccharomyces cerevisiae,” FEBS Letters, vol. 333, no. 1-2, pp. 169–174, 1993. View at Publisher · View at Google Scholar · View at Scopus
  35. M. Thumm, R. Egner, B. Koch et al., “Isolation of autophagocytosis mutants of Saccharomyces cerevisiae,” FEBS Letters, vol. 349, no. 2, pp. 275–280, 1994. View at Publisher · View at Google Scholar · View at Scopus
  36. T. M. Harding, K. A. Morano, S. V. Scott, and D. J. Klionsky, “Isolation and characterization of yeast mutants in the cytoplasm to vacuole protein targeting pathway,” The Journal of Cell Biology, vol. 131, no. 3, pp. 591–602, 1995. View at Publisher · View at Google Scholar · View at Scopus
  37. D. J. Klionsky, J. M. Cregg, W. A. Dunn Jr. et al., “A unified nomenclature for yeast autophagy-related genes,” Developmental Cell, vol. 5, no. 4, pp. 539–545, 2003. View at Publisher · View at Google Scholar · View at Scopus
  38. G. Juhász, G. Csikós, R. Sinka, M. Erdélyi, and M. Sass, “The Drosophila homolog of Aut1 is essential for autophagy and development,” FEBS Letters, vol. 543, no. 1–3, pp. 154–158, 2003. View at Publisher · View at Google Scholar · View at Scopus
  39. K. Suzuki, Y. Kubota, T. Sekito, and Y. Ohsumi, “Hierarchy of Atg proteins in pre-autophagosomal structure organization,” Genes to Cells, vol. 12, no. 2, pp. 209–218, 2007. View at Publisher · View at Google Scholar · View at Scopus
  40. E. Itakura and N. Mizushima, “Characterization of autophagosome formation site by a hierarchical analysis of mammalian Atg proteins,” Autophagy, vol. 6, no. 6, pp. 764–776, 2010. View at Publisher · View at Google Scholar · View at Scopus
  41. Q. Lu, P. Yang, X. Huang et al., “The WD40 repeat PtdIns(3)P-binding protein EPG-6 regulates progression of omegasomes to autophagosomes,” Developmental Cell, vol. 21, no. 2, pp. 343–357, 2011. View at Publisher · View at Google Scholar · View at Scopus
  42. I. Koyama-Honda, E. Itakura, T. K. Fujiwara, and N. Mizushima, “Temporal analysis of recruitment of mammalian ATG proteins to the autophagosome formation site,” Autophagy, vol. 9, no. 10, pp. 1491–1499, 2013. View at Publisher · View at Google Scholar
  43. K. Suzuki, M. Akioka, C. Kondo-Kakuta, H. Yamamoto, and Y. Ohsumi, “Fine mapping of autophagy-related proteins during autophagosome formation in Saccharomyces cerevisiae,” Journal of Cell Science, vol. 126, part 11, pp. 2534–2544, 2013. View at Google Scholar
  44. N. Mizushima, “The role of the Atg1/ULK1 complex in autophagy regulation,” Current Opinion in Cell Biology, vol. 22, no. 2, pp. 132–139, 2010. View at Publisher · View at Google Scholar · View at Scopus
  45. Y.-Y. Chang and T. P. Neufeld, “An Atg1/Atg13 complex with multiple roles in TOR-mediated autophagy regulation,” Molecular Biology of the Cell, vol. 20, no. 7, pp. 2004–2014, 2009. View at Publisher · View at Google Scholar · View at Scopus
  46. P. Nagy, M. Karpati, A. Varga et al., “Atg17/FIP200 localizes to perilysosomal Ref(2)P aggregates and promotes autophagy by activation of Atg1 in Drosophila,” Autophagy, vol. 10, no. 3, pp. 453–467, 2014. View at Google Scholar
  47. R. C. Scott, G. Juhász, and T. P. Neufeld, “Direct induction of autophagy by atg1 inhibits cell growth and induces apoptotic cell death,” Current Biology, vol. 17, no. 1, pp. 1–11, 2007. View at Publisher · View at Google Scholar · View at Scopus
  48. J. H. Stack, D. B. DeWald, K. Takegawa, and S. D. Emr, “Vesicle-mediated protein transport: regulatory interactions between the Vps15 protein kinase and the Vps34 PtdIns 3-kinase essential for protein sorting to the vacuole in yeast,” The Journal of Cell Biology, vol. 129, no. 2, pp. 321–334, 1995. View at Google Scholar · View at Scopus
  49. E. Itakura, C. Kishi, K. Inoue, and N. Mizushima, “Beclin 1 forms two distinct phosphatidylinositol 3-kinase complexes with mammalian Atg14 and UVRAG,” Molecular Biology of the Cell, vol. 19, no. 12, pp. 5360–5372, 2008. View at Publisher · View at Google Scholar · View at Scopus
  50. X. Li, L. He, K. H. Che et al., “Imperfect interface of Beclin1 coiled-coil domain regulates homodimer and heterodimer formation with Atg14L and UVRAG,” Nature Communications, vol. 3, article 662, 2012. View at Publisher · View at Google Scholar · View at Scopus
  51. G. Juhász, J. H. Hill, Y. Yan et al., “The class III PI(3)K Vps34 promotes autophagy and endocytosis but not TOR signaling in Drosophila,” The Journal of Cell Biology, vol. 181, no. 4, pp. 655–666, 2008. View at Publisher · View at Google Scholar · View at Scopus
  52. P. Musiwaro, M. Smith, M. Manifava, S. A. Walker, and N. T. Ktistakis, “Characteristics and requirements of basal autophagy in HEK 293 cells,” Autophagy, vol. 9, no. 9, pp. 1407–1417, 2013. View at Publisher · View at Google Scholar
  53. K. Devereaux, C. Dall'armi, A. Alcazar-Roman et al., “Regulation of mammalian autophagy by class II and III PI 3-kinases through PI3P synthesis,” PloS ONE, vol. 8, no. 10, Article ID e76405, 2013. View at Google Scholar
  54. K. Lindmo, A. Brech, K. D. Finley et al., “The PI 3-kinase regulator Vps15 is required for autophagic clearance of protein aggregates,” Autophagy, vol. 4, no. 4, pp. 500–506, 2008. View at Google Scholar · View at Scopus
  55. B. V. Shravage, J. H. Hill, C. M. Powers, L. Wu, and E. H. Baehrecke, “Atg6 is required for multiple vesicle trafficking pathways and hematopoiesis in Drosophila,” Development, vol. 140, no. 6, pp. 1321–1329, 2013. View at Publisher · View at Google Scholar
  56. A. Banreti, T. Lukacsovich, G. Csikos, M. Erdelyi, and M. Sass, “PP2A regulates autophagy in two alternative ways in Drosophila,” Autophagy, vol. 8, no. 4, pp. 623–636, 2012. View at Publisher · View at Google Scholar
  57. K. Pircs, P. Nagy, A. Varga et al., “Advantages and limitations of different p62-based assays for estimating autophagic activity in Drosophila,” PloS ONE, vol. 7, no. 8, Article ID e44214, 2012. View at Google Scholar
  58. S. Takats, K. Pircs, P. Nagy et al., “Interaction of the HOPS complex with Syntaxin 17 mediates autophagosome clearance in Drosophila,” Molecular Biology of the Cell, vol. 25, no. 8, pp. 1338–1354, 2014. View at Publisher · View at Google Scholar
  59. P. Lorincz, Z. Lakatos, T. Maruzs, Z. Szatmari, V. Kis, and M. Sass, “Atg6/UVRAG/Vps34-containing lipid kinase complex is required for receptor downregulation through endolysosomal degradation and epithelial polarity during Drosophila wing development,” BioMed Research International. In press.
  60. T. Proikas-Cezanne, S. Ruckerbauer, Y.-D. Stierhof, C. Berg, and A. Nordheim, “Human WIPI-1 puncta-formation: a novel assay to assess mammalian autophagy,” FEBS Letters, vol. 581, no. 18, pp. 3396–3404, 2007. View at Publisher · View at Google Scholar · View at Scopus
  61. H. E. J. Polson, J. De Lartigue, D. J. Rigden et al., “Mammalian Atg18 (WIPI2) localizes to omegasome-anchored phagophores and positively regulates LC3 lipidation,” Autophagy, vol. 6, no. 4, pp. 506–522, 2010. View at Publisher · View at Google Scholar · View at Scopus
  62. R. C. Scott, O. Schuldiner, and T. P. Neufeld, “Role and regulation of starvation-induced autophagy in the Drosophila fat body,” Developmental Cell, vol. 7, no. 2, pp. 167–178, 2004. View at Publisher · View at Google Scholar · View at Scopus
  63. E. L. Axe, S. A. Walker, M. Manifava et al., “Autophagosome formation from membrane compartments enriched in phosphatidylinositol 3-phosphate and dynamically connected to the endoplasmic reticulum,” The Journal of Cell Biology, vol. 182, no. 4, pp. 685–701, 2008. View at Publisher · View at Google Scholar · View at Scopus
  64. Y. Tian, Z. Li, W. Hu et al., “C. elegans screen identifies autophagy genes specific to multicellular organisms,” Cell, vol. 141, no. 6, pp. 1042–1055, 2010. View at Publisher · View at Google Scholar · View at Scopus
  65. M. I. Molejon, A. Ropolo, A. L. Re, V. Boggio, and M. I. Vaccaro, “The VMP1-Beclin 1 interaction regulates autophagy induction,” Scientific Reports, vol. 3, article 1055, 2013. View at Google Scholar
  66. F. Bard, L. Casano, A. Mallabiabarrena et al., “Functional genomics reveals genes involved in protein secretion and Golgi organization,” Nature, vol. 439, no. 7076, pp. 604–607, 2006. View at Publisher · View at Google Scholar · View at Scopus
  67. H. Yamamoto, S. Kakuta, T. M. Watanabe et al., “Atg9 vesicles are an important membrane source during early steps of autophagosome formation,” The Journal of Cell Biology, vol. 198, no. 2, pp. 219–233, 2012. View at Publisher · View at Google Scholar
  68. A. Orsi, M. Razi, H. Dooley et al., “Dynamic and transient interactions of Atg9 with autophagosomes, but not membrane integration, is required for autophagy,” Molecular Biology of the Cell, vol. 23, no. 10, pp. 1860–1873, 2012. View at Publisher · View at Google Scholar
  69. C. Puri, M. Renna, C. F. Bento, K. Moreau, and D. C. Rubinsztein, “Diverse autophagosome membrane sources coalesce in recycling endosomes,” Cell, vol. 154, no. 6, pp. 1285–1299, 2013. View at Publisher · View at Google Scholar
  70. S. A. Tooze, “Current views on the source of the autophagosome membrane,” Essays in Biochemistry, vol. 55, pp. 29–38, 2013. View at Publisher · View at Google Scholar
  71. G. Juhasz and T. P. Neufeld, “Autophagy: a forty-year search for a missing membrane source,” PLoS Biology, vol. 4, no. 2, p. e36, 2006. View at Publisher · View at Google Scholar · View at Scopus
  72. A. L. Kovács, Z. Pálfia, G. Réz, T. Vellai, and J. Kovács, “Sequestration revisited: integrating traditional electron microscopy, de novo assembly and new results,” Autophagy, vol. 3, no. 6, pp. 655–662, 2007. View at Google Scholar · View at Scopus
  73. P. Nagy, A. Varga, K. Pircs, K. Hegedus, and G. Juhasz, “Myc-driven overgrowth requires unfolded protein response-mediated induction of autophagy and antioxidant responses in Drosophila melanogaster,” PLoS Genetics, vol. 9, no. 8, Article ID e1003664, 2013. View at Google Scholar
  74. P. Low, A. Varga, K. Pircs et al., “Impaired proteasomal degradation enhances autophagy via hypoxia signaling in Drosophila,” BMC Cell Biology, vol. 14, no. 1, article 29, 2013. View at Google Scholar
  75. P. Nagy, K. Hegedus, K. Pircs, A. Varga, and G. Juhasz, “Different effects of Atg2 and Atg18 mutations on Atg8a and Atg9 trafficking during starvation in Drosophila,” FEBS Letters, vol. 588, no. 3, pp. 408–413, 2014. View at Publisher · View at Google Scholar
  76. F. Reggiori, K. A. Tucker, P. E. Stromhaug, and D. J. Klionsky, “The Atg1-Atg13 complex regulates Atg9 and Atg23 retrieval transport from the pre-autophagosomal structure,” Developmental Cell, vol. 6, no. 1, pp. 79–90, 2004. View at Publisher · View at Google Scholar · View at Scopus
  77. Y. Ichimura, T. Kirisako, T. Takao et al., “A ubiquitin-like system mediates protein lipidation,” Nature, vol. 408, no. 6811, pp. 488–492, 2000. View at Publisher · View at Google Scholar · View at Scopus
  78. M. Matsushita, N. N. Suzuki, K. Obara, Y. Fujioka, Y. Ohsumi, and F. Inagaki, “Structure of Atg5·Atg16, a complex essential for autophagy,” Journal of Biological Chemistry, vol. 282, no. 9, pp. 6763–6772, 2007. View at Publisher · View at Google Scholar · View at Scopus
  79. D. J. Klionsky, F. C. Abdalla, H. Abeliovich et al., “Guidelines for the use and interpretation of assays for monitoring autophagy,” Autophagy, vol. 8, no. 4, pp. 445–544, 2012. View at Publisher · View at Google Scholar
  80. S. Takats, P. Nagy, A. Varga et al., “Autophagosomal Syntaxin17-dependent lysosomal degradation maintains neuronal function in Drosophila,” The Journal of Cell Biology, vol. 201, no. 4, pp. 531–539, 2013. View at Publisher · View at Google Scholar
  81. E. Itakura, C. Kishi-Itakura, and N. Mizushima, “The hairpin-type tail-anchored SNARE syntaxin 17 targets to autophagosomes for fusion with endosomes/lysosomes,” Cell, vol. 151, no. 6, pp. 1256–1269, 2012. View at Publisher · View at Google Scholar
  82. K. Hegedus, S. Takats, A. L. Kovacs, and G. Juhasz, “Evolutionarily conserved role and physiological relevance of a STX17/Syx17 (syntaxin 17)-containing SNARE complex in autophagosome fusion with endosomes and lysosomes,” Autophagy, vol. 9, no. 10, pp. 1642–1646, 2013. View at Publisher · View at Google Scholar
  83. T. Kobayashi, K. Suzuki, and Y. Ohsumi, “Autophagosome formation can be achieved in the absence of Atg18 by expressing engineered PAS-targeted Atg2,” FEBS Letters, vol. 586, no. 16, pp. 2473–2478, 2012. View at Publisher · View at Google Scholar
  84. A. K. G. Velikkakath, T. Nishimura, E. Oita, N. Ishihara, and N. Mizushima, “Mammalian Atg2 proteins are essential for autophagosome formation and important for regulation of size and distribution of lipid droplets,” Molecular Biology of the Cell, vol. 23, no. 5, pp. 896–909, 2012. View at Publisher · View at Google Scholar · View at Scopus
  85. D. Denton, B. Shravage, R. Simin et al., “Autophagy, not apoptosis, is essential for midgut cell death in Drosophila,” Current Biology, vol. 19, no. 20, pp. 1741–1746, 2009. View at Publisher · View at Google Scholar · View at Scopus
  86. C.-W. Wang, P. E. Stromhaug, J. Shima, and D. J. Klionsky, “The Ccz1-Mon1 protein complex is required for the late step of multiple vacuole delivery pathways,” Journal of Biological Chemistry, vol. 277, no. 49, pp. 47917–47927, 2002. View at Publisher · View at Google Scholar · View at Scopus
  87. T. E. Rusten, T. Vaccari, K. Lindmo et al., “ESCRTs and Fab1 regulate distinct steps of autophagy,” Current Biology, vol. 17, no. 20, pp. 1817–1825, 2007. View at Publisher · View at Google Scholar · View at Scopus
  88. P. Jiang, T. Nishimura, Y. Sakamaki et al., “The HOPS complex mediates autophagosome-lysosome fusion through interaction with syntaxin 17,” Molecular Biology of the Cell, vol. 25, no. 8, pp. 1327–1337, 2014. View at Publisher · View at Google Scholar
  89. T. Noda and Y. Ohsumi, “Tor, a phosphatidylinositol kinase homologue, controls autophagy in yeast,” Journal of Biological Chemistry, vol. 273, no. 7, pp. 3963–3966, 1998. View at Publisher · View at Google Scholar · View at Scopus
  90. T. P. Neufeld, “TOR-dependent control of autophagy: biting the hand that feeds,” Current Opinion in Cell Biology, vol. 22, no. 2, pp. 157–168, 2010. View at Publisher · View at Google Scholar · View at Scopus
  91. N. Hosokawa, T. Hara, T. Kaizuka et al., “Nutrient-dependent mTORCl association with the ULK1-Atg13-FIP200 complex required for autophagy,” Molecular Biology of the Cell, vol. 20, no. 7, pp. 1981–1991, 2009. View at Publisher · View at Google Scholar · View at Scopus
  92. C. H. Jung, C. B. Jun, S.-H. Ro et al., “ULK-Atg13-FIP200 complexes mediate mTOR signaling to the autophagy machinery,” Molecular Biology of the Cell, vol. 20, no. 7, pp. 1992–2003, 2009. View at Publisher · View at Google Scholar · View at Scopus
  93. G. Juhasz, “Interpretation of bafilomycin, pH neutralizing or protease inhibitor treatments in autophagic flux experiments: novel considerations,” Autophagy, vol. 8, no. 12, pp. 1875–1876, 2012. View at Publisher · View at Google Scholar
  94. M. Li, B. Khambu, H. Zhang et al., “Suppression of lysosome function induces autophagy via a feedback down-regulation of MTOR complex 1 (MTORC1) activity,” The Journal of Biological Chemistry, vol. 288, no. 50, pp. 35769–35780, 2013. View at Publisher · View at Google Scholar
  95. C. H. Jung, M. Seo, N. M. Otto, and D.-H. Kim, “ULK1 inhibits the kinase activity of mTORC1 and cell proliferation,” Autophagy, vol. 7, no. 10, pp. 1212–1221, 2011. View at Publisher · View at Google Scholar · View at Scopus
  96. T. E. Rusten, K. Lindmo, G. Juhász et al., “Programmed autophagy in the Drosophila fat body is induced by ecdysone through regulation of the PI3K Pathway,” Developmental Cell, vol. 7, no. 2, pp. 179–192, 2004. View at Publisher · View at Google Scholar · View at Scopus
  97. L. Y. Cheng, A. P. Bailey, S. J. Leevers, T. J. Ragan, P. C. Driscoll, and A. P. Gould, “Anaplastic lymphoma kinase spares organ growth during nutrient restriction in drosophila,” Cell, vol. 146, no. 3, pp. 435–447, 2011. View at Publisher · View at Google Scholar · View at Scopus
  98. F. O'Farrell, S. Wang, N. Katheder, T. E. Rusten, and C. Samakovlis, “Two-tiered control of epithelial growth and autophagy by the insulin receptor and the ret-like receptor, stitcher,” PLoS Biology, vol. 11, no. 7, Article ID e1001612, 2013. View at Google Scholar
  99. M. Slaidina, R. Delanoue, S. Gronke, L. Partridge, and P. Léopold, “A Drosophila insulin-like peptide promotes growth during nonfeeding states,” Developmental Cell, vol. 17, no. 6, pp. 874–884, 2009. View at Publisher · View at Google Scholar · View at Scopus
  100. B. Tysell and F. M. Butterworth, “Different rate of protein granule formation in the larval fat body of Drosophila melanogaster,” Journal of Insect Physiology, vol. 24, no. 3, pp. 201–206, 1978. View at Google Scholar · View at Scopus
  101. T. M. Rizki and R. M. Rizki, “Developmental biology and genetics of adipose tissue of the Drosophila larva,” Egyptian Journal of Genetics and Cytology, vol. 1, pp. 173–184, 1972. View at Google Scholar
  102. M. Jindra, S. R. Palli, and L. M. Riddiford, “The juvenile hormone signaling pathway in insect development,” Annual Review of Entomology, vol. 58, pp. 181–204, 2013. View at Publisher · View at Google Scholar
  103. G. Juhász, L. G. Puskás, O. Komonyi et al., “Gene expression profiling identifies FKBP39 as an inhibitor of autophagy in larval Drosophila fat body,” Cell Death and Differentiation, vol. 14, no. 6, pp. 1181–1190, 2007. View at Publisher · View at Google Scholar · View at Scopus
  104. B. Erdi, P. Nagy, A. Zvara et al., “Loss of the starvation-induced gene Rack1 leads to glycogen deficiency and impaired autophagic responses in Drosophila,” Autophagy, vol. 8, no. 7, pp. 1124–1135, 2012. View at Publisher · View at Google Scholar
  105. T. Sigmond, J. Fehér, A. Baksa et al., “Qualitative and quantitative characterization of autophagy in Caenorhabditis elegans by electron microscopy,” Methods in Enzymology, vol. 451, pp. 467–491, 2008. View at Google Scholar · View at Scopus
  106. L. Cherbas, X. Hu, I. Zhimulev, E. Belyaeva, and P. Cherbas, “EcR isoforms in Drosophila: testing tissue-specific requirements by targeted blockade and rescue,” Development, vol. 130, no. 2, pp. 271–284, 2003. View at Publisher · View at Google Scholar · View at Scopus
  107. J. R. Aguila, J. Suszko, A. G. Gibbs, and D. K. Hoshizaki, “The role of larval fat cells in adult Drosophila melanogaster,” Journal of Experimental Biology, vol. 210, no. 6, pp. 956–963, 2007. View at Publisher · View at Google Scholar · View at Scopus
  108. F. M. Butterworth, L. Emerson, and E. M. Rasch, “Maturation and degeneration of the fat body in the Drosophila larva and pupa as revealed by morphometric analysis,” Tissue and Cell, vol. 20, no. 2, pp. 255–268, 1988. View at Google Scholar · View at Scopus
  109. F. Akdemir, R. Farkaš, P. Chen et al., “Autophagy occurs upstream or parallel to the apoptosome during histolytic cell death,” Development, vol. 133, no. 8, pp. 1457–1465, 2006. View at Publisher · View at Google Scholar · View at Scopus
  110. V. P. Yin and C. S. Thummel, “A balance between the diap1 death inhibitor and reaper and hid death inducers controls steroid-triggered cell death in Drosophila,” Proceedings of the National Academy of Sciences of the United States of America, vol. 101, no. 21, pp. 8022–8027, 2004. View at Publisher · View at Google Scholar · View at Scopus
  111. D. L. Berry and E. H. Baehrecke, “Growth arrest and autophagy are required for salivary gland cell degradation in Drosophila,” Cell, vol. 131, no. 6, pp. 1137–1148, 2007. View at Publisher · View at Google Scholar · View at Scopus
  112. C. Jiang, E. H. Baehrecke, and C. S. Thummel, “Steroid regulated programmed cell death during Drosophila metamorphosis,” Development, vol. 124, no. 22, pp. 4673–4683, 1997. View at Google Scholar · View at Scopus
  113. G. Juhász, B. Érdi, M. Sass, and T. P. Neufeld, “Atg7-dependent autophagy promotes neuronal health, stress tolerance, and longevity but is dispensable for metamorphosis in Drosophila,” Genes and Development, vol. 21, no. 23, pp. 3061–3066, 2007. View at Publisher · View at Google Scholar · View at Scopus
  114. C.-Y. Lee and E. H. Baehrecke, “Steroid regulation of autophagic programmed cell death during development,” Development, vol. 128, no. 8, pp. 1443–1445, 2001. View at Google Scholar · View at Scopus
  115. T. K. Chang, B. V. Shravage, S. D. Hayes et al., “Uba1 functions in Atg7- and Atg3-independent autophagy,” Nature Cell Biology, vol. 15, no. 9, pp. 1067–1078, 2013. View at Publisher · View at Google Scholar
  116. G. Juhász and M. Sass, “Hid can induce, but is not required for autophagy in polyploid larval Drosophila tissues,” European Journal of Cell Biology, vol. 84, no. 4, pp. 491–502, 2005. View at Publisher · View at Google Scholar · View at Scopus
  117. J. Broadus, J. R. McCabe, B. Endrizzi, C. S. Thummel, and C. T. Woodard, “The Drosophila βFTZ-F1 orphan nuclear receptor provides competence for stage-specific responses to the steroid hormone ecdysone,” Molecular Cell, vol. 3, no. 2, pp. 143–149, 1999. View at Publisher · View at Google Scholar · View at Scopus
  118. C.-Y. Lee, B. A. K. Cooksey, and E. H. Baehrecke, “Steroid regulation of midgut cell death during Drosophila development,” Developmental Biology, vol. 250, no. 1, pp. 101–111, 2002. View at Publisher · View at Google Scholar · View at Scopus
  119. X. Qu, Z. Zou, Q. Sun et al., “Autophagy gene-dependent clearance of apoptotic cells during embryonic development,” Cell, vol. 128, no. 5, pp. 931–946, 2007. View at Publisher · View at Google Scholar · View at Scopus
  120. M. Kim, H. L. Park, H. W. Park et al., “Drosophila Fip200 is an essential regulator of autophagy that attenuates both growth and aging,” Autophagy, vol. 9, no. 8, 2013. View at Google Scholar
  121. G. Lee, C. Liang, G. Park, C. Jang, J. U. Jung, and J. Chung, “UVRAG is required for organ rotation by regulating Notch endocytosis in Drosophila,” Developmental Biology, vol. 356, no. 2, pp. 588–597, 2011. View at Publisher · View at Google Scholar · View at Scopus
  122. A. Simonsen, R. C. Cumming, A. Brech, P. Isakson, D. R. Schubert, and K. D. Finley, “Promoting basal levels of autophagy in the nervous system enhances longevity and oxidant resistance in adult Drosophila,” Autophagy, vol. 4, no. 2, pp. 176–184, 2008. View at Google Scholar · View at Scopus
  123. I. P. Nezis, B. V. Shravage, A. P. Sagona et al., “Autophagic degradation of dBruce controls DNA fragmentation in nurse cells during late Drosophila melanogaster oogenesis,” The Journal of Cell Biology, vol. 190, no. 4, pp. 523–531, 2010. View at Publisher · View at Google Scholar · View at Scopus
  124. J. S. Peterson and K. McCall, “Combined inhibition of autophagy and caspases fails to prevent developmental nurse cell death in the Drosophila melanogaster ovary,” PloS ONE, vol. 8, no. 9, Article ID e76046, 2013. View at Google Scholar
  125. B. P. Bass, E. A. Tanner, D. Mateos San Martín et al., “Cell-autonomous requirement for DNaseII in nonapoptotic cell death,” Cell Death and Differentiation, vol. 16, no. 10, pp. 1362–1371, 2009. View at Publisher · View at Google Scholar · View at Scopus
  126. Y.-C. C. Hou, S. Chittaranjan, S. G. Barbosa, K. McCall, and S. M. Gorski, “Effector caspase Dcp-1 and IAP protein Bruce regulate starvation-induced autophagy during Drosophila melanogaster oogenesis,” The Journal of Cell Biology, vol. 182, no. 6, pp. 1127–1139, 2008. View at Publisher · View at Google Scholar · View at Scopus
  127. J. M. I. Barth, J. Szabad, E. Hafen, and K. Köhler, “Autophagy in Drosophila ovaries is induced by starvation and is required for oogenesis,” Cell Death and Differentiation, vol. 18, no. 6, pp. 915–924, 2011. View at Publisher · View at Google Scholar · View at Scopus
  128. L. P. Nezis, T. Lamark, A. D. Velentzas et al., “Cell death during Drosophila melanogaster early oogenesis is mediated through autophagy,” Autophagy, vol. 5, no. 3, pp. 298–302, 2009. View at Publisher · View at Google Scholar · View at Scopus
  129. J. M. Barth, E. Hafen, and K. Kohler, “The lack of autophagy triggers precocious activation of Notch signaling during Drosophila oogenesis,” BMC Developmental Biology, vol. 12, article 35, 2012. View at Google Scholar
  130. N. Mohseni, S. C. McMillan, R. Chaudhary, J. Mok, and B. H. Reed, “Autophagy promotes caspase-dependent cell death during Drosophila development,” Autophagy, vol. 5, no. 3, pp. 329–338, 2009. View at Publisher · View at Google Scholar · View at Scopus
  131. O. Cormier, N. Mohseni, I. Voytyuk, and B. H. Reed, “Autophagy can promote but is not required for epithelial cell extrusion in the amnioserosa of the Drosophila embryo,” Autophagy, vol. 8, no. 2, pp. 252–264, 2012. View at Publisher · View at Google Scholar · View at Scopus
  132. P. P. Toh, S. Luo, F. M. Menzies, T. Rasko, E. E. Wanker, and D. C. Rubinsztein, “Myc inhibition impairs autophagosome formation,” Human Molecular Genetics, vol. 22, no. 25, pp. 5237–5248, 2013. View at Publisher · View at Google Scholar
  133. L. S. Hart, J. T. Cunningham, T. Datta et al., “ER stress-mediated autophagy promotes Myc-dependent transformation and tumor growth,” The Journal of Clinical Investigation, vol. 122, no. 12, pp. 4621–4634, 2012. View at Publisher · View at Google Scholar
  134. E. Bier, “Drosophila, the golden bug, emerges as a tool for human genetics,” Nature Reviews Genetics, vol. 6, no. 1, pp. 9–23, 2005. View at Publisher · View at Google Scholar · View at Scopus
  135. V. Deretic and B. Levine, “Autophagy, immunity, and microbial adaptations,” Cell Host and Microbe, vol. 5, no. 6, pp. 527–549, 2009. View at Publisher · View at Google Scholar · View at Scopus
  136. K. Kirkegaard, M. P. Taylor, and W. T. Jackson, “Cellular autophagy: surrender, avoidance and subversion by microorganisms,” Nature Reviews Microbiology, vol. 2, no. 4, pp. 301–314, 2004. View at Publisher · View at Google Scholar · View at Scopus
  137. R. H. Moy and S. Cherry, “Antimicrobial autophagy: a conserved innate immune response in Drosophila,” Journal of Innate Immunity, vol. 5, no. 5, pp. 444–455, 2013. View at Publisher · View at Google Scholar
  138. B. Lemaitre and J. Hoffmann, “The host defense of Drosophila melanogaster,” Annual Review of Immunology, vol. 25, pp. 697–743, 2007. View at Publisher · View at Google Scholar · View at Scopus
  139. D. Ferrandon, J.-L. Imler, C. Hetru, and J. A. Hoffmann, “The Drosophila systemic immune response: sensing and signalling during bacterial and fungal infections,” Nature Reviews Immunology, vol. 7, no. 11, pp. 862–874, 2007. View at Publisher · View at Google Scholar · View at Scopus
  140. H. Agaisse and N. Perrimon, “The roles of JAK/STAT signaling in Drosophila immune responses,” Immunological Reviews, vol. 198, pp. 72–82, 2004. View at Publisher · View at Google Scholar · View at Scopus
  141. J. Xu, G. Grant, L. R. Sabin et al., “Transcriptional pausing controls a rapid antiviral innate immune response in Drosophila,” Cell Host & Microbe, vol. 12, no. 4, pp. 531–543, 2012. View at Google Scholar
  142. V. Deretic, “Autophagy as an innate immunity paradigm: expanding the scope and repertoire of pattern recognition receptors,” Current Opinion in Immunology, vol. 24, no. 1, pp. 21–31, 2012. View at Publisher · View at Google Scholar · View at Scopus
  143. S. Akira, S. Uematsu, and O. Takeuchi, “Pathogen recognition and innate immunity,” Cell, vol. 124, no. 4, pp. 783–801, 2006. View at Publisher · View at Google Scholar · View at Scopus
  144. M. A. Delgado, R. A. Elmaoued, A. S. Davis, G. Kyei, and V. Deretic, “Toll-like receptors control autophagy,” The EMBO Journal, vol. 27, no. 7, pp. 1110–1121, 2008. View at Publisher · View at Google Scholar · View at Scopus
  145. S. Kurata, “Peptidoglycan recognition proteins in Drosophila immunity,” Developmental and Comparative Immunology, vol. 42, no. 1, pp. 36–41, 2014. View at Google Scholar
  146. J. Royet, “Drosophila melanogaster innate immunity: an emerging role for peptidoglycan recognition proteins in bacteria detection,” Cellular and Molecular Life Sciences, vol. 61, no. 5, pp. 537–546, 2004. View at Publisher · View at Google Scholar · View at Scopus
  147. M. G. Gutierrez, S. S. Master, S. B. Singh, G. A. Taylor, M. I. Colombo, and V. Deretic, “Autophagy is a defense mechanism inhibiting BCG and Mycobacterium tuberculosis survival in infected macrophages,” Cell, vol. 119, no. 6, pp. 753–766, 2004. View at Publisher · View at Google Scholar · View at Scopus
  148. Y. M. Ling, M. H. Shaw, C. Ayala et al., “Vacuolar and plasma membrane stripping and autophagic elimination of Toxoplasma gondii in primed effector macrophages,” The Journal of Experimental Medicine, vol. 203, no. 9, pp. 2063–2071, 2006. View at Publisher · View at Google Scholar · View at Scopus
  149. I. Nakagawa, A. Amano, N. Mizushima et al., “Autophagy defends cells against invading group A Streptococcus,” Science, vol. 306, no. 5698, pp. 1037–1040, 2004. View at Publisher · View at Google Scholar · View at Scopus
  150. A. Orvedahl, S. MacPherson, R. Sumpter Jr., Z. Tallóczy, Z. Zou, and B. Levine, “Autophagy protects against Sindbis virus infection of the central nervous system,” Cell Host and Microbe, vol. 7, no. 2, pp. 115–127, 2010. View at Publisher · View at Google Scholar · View at Scopus
  151. S. Shelly, N. Lukinova, S. Bambina, A. Berman, and S. Cherry, “Autophagy is an essential component of Drosophila immunity against vesicular stomatitis virus,” Immunity, vol. 30, no. 4, pp. 588–598, 2009. View at Publisher · View at Google Scholar · View at Scopus
  152. B. Yordy and A. Iwasaki, “Cell type-dependent requirement of autophagy in HSV-1 antiviral defense,” Autophagy, vol. 9, no. 2, pp. 236–238, 2013. View at Publisher · View at Google Scholar
  153. Y. Yoshikawa, M. Ogawa, T. Hain et al., “Listeria monocytogenes ActA-mediated escape from autophagic recognition,” Nature Cell Biology, vol. 11, no. 10, pp. 1233–1240, 2009. View at Publisher · View at Google Scholar · View at Scopus
  154. Y. T. Zheng, S. Shahnazari, A. Brech, T. Lamark, T. Johansen, and J. H. Brumell, “The adaptor protein p62/SQSTM1 targets invading bacteria to the autophagy pathway,” Journal of Immunology, vol. 183, no. 9, pp. 5909–5916, 2009. View at Publisher · View at Google Scholar · View at Scopus
  155. P. S. Manzanillo, J. S. Ayres, R. O. Watson et al., “The ubiquitin ligase parkin mediates resistance to intracellular pathogens,” Nature, vol. 501, no. 7468, pp. 512–516, 2013. View at Google Scholar
  156. B. E. Mansfield, M. S. Dionne, D. S. Schneider, and N. E. Freitag, “Exploration of host-pathogen interactions using Listeria monocytogenes and Drosophila melanogaster,” Cellular Microbiology, vol. 5, no. 12, pp. 901–911, 2003. View at Publisher · View at Google Scholar · View at Scopus
  157. T. Yano, S. Mita, H. Ohmori et al., “Autophagic control of listeria through intracellular innate immune recognition in drosophila,” Nature Immunology, vol. 9, no. 8, pp. 908–916, 2008. View at Publisher · View at Google Scholar · View at Scopus
  158. L. Dortet, S. Mostowy, A. S. Louaka et al., “Recruitment of the major vault protein by inlk: a listeria monocytogenes strategy to avoid autophagy,” PLoS Pathogens, vol. 7, no. 8, Article ID e1002168, 2011. View at Publisher · View at Google Scholar · View at Scopus
  159. S. Kurata, “Extracellular and intracellular pathogen recognition by Drosophila PGRP-LE and PGRP-LC,” International Immunology, vol. 22, no. 3, Article ID dxp128, pp. 143–148, 2010. View at Publisher · View at Google Scholar · View at Scopus
  160. A. Takehana, T. Yano, S. Mita, A. Kotani, Y. Oshima, and S. Kurata, “Peptidoglycan recognition protein (PGRP)-LE and PGRP-LC act synergistically in Drosophila immunity,” EMBO Journal, vol. 23, no. 23, pp. 4690–4700, 2004. View at Publisher · View at Google Scholar · View at Scopus
  161. T. Kaneko, T. Yano, K. Aggarwal et al., “PGRP-LC and PGRP-LE have essential yet distinct functions in the drosophila immune response to monomeric DAP-type peptidoglycan,” Nature Immunology, vol. 7, no. 7, pp. 715–723, 2006. View at Publisher · View at Google Scholar · View at Scopus
  162. A. Goto, T. Yano, J. Terashima, S. Iwashita, Y. Oshima, and S. Kurata, “Cooperative regulation of the induction of the novel antibacterial listericin by peptidoglycan recognition protein LE and the JAK-STAT pathway,” Journal of Biological Chemistry, vol. 285, no. 21, pp. 15731–15738, 2010. View at Publisher · View at Google Scholar · View at Scopus
  163. D. Voronin, D. A. Cook, A. Steven, and M. J. Taylor, “Autophagy regulates Wolbachia populations across diverse symbiotic associations,” Proceedings of the National Academy of Sciences of the United States of America, vol. 109, no. 25, pp. E1638–E1646, 2012. View at Publisher · View at Google Scholar
  164. X. H. Liang, L. K. Kleeman, H. H. Jiang et al., “Protection against fatal sindbis virus encephalitis by Beclin, a novel Bcl-2-interacting protein,” Journal of Virology, vol. 72, no. 11, pp. 8586–8596, 1998. View at Google Scholar · View at Scopus
  165. Z. Surviladze, R. T. Sterk, S. A. DeHaro, and M. A. Ozbun, “Cellular entry of human papillomavirus type 16 involves activation of the phosphatidylinositol 3-kinase/Akt/mTOR pathway and inhibition of autophagy,” Journal of Virology, vol. 87, no. 5, pp. 2508–2517, 2013. View at Publisher · View at Google Scholar
  166. G. R. Campbell and S. A. Spector, “Vitamin D inhibits human immunodeficiency virus type 1 and Mycobacterium tuberculosis infection in macrophages through the induction of autophagy,” PLoS Pathogens, vol. 8, no. 5, Article ID e1002689, 2012. View at Google Scholar
  167. M. Nakamoto, R. H. Moy, J. Xu et al., “Virus recognition by Toll-7 activates antiviral autophagy in Drosophila,” Immunity, vol. 36, no. 4, pp. 658–667, 2012. View at Publisher · View at Google Scholar · View at Scopus
  168. F. Leulier and B. Lemaitre, “Toll-like receptors—taking an evolutionary approach,” Nature Reviews Genetics, vol. 9, no. 3, pp. 165–178, 2008. View at Publisher · View at Google Scholar · View at Scopus
  169. Y. Xu, C. Jagannath, X.-D. Liu, A. Sharafkhaneh, K. E. Kolodziejska, and N. T. Eissa, “Toll-like receptor 4 is a sensor for autophagy associated with innate immunity,” Immunity, vol. 27, no. 1, pp. 135–144, 2007. View at Publisher · View at Google Scholar · View at Scopus
  170. C.-S. Shi and J. H. Kehrl, “MyD88 and Trif target Beclin 1 to trigger autophagy in macrophages,” Journal of Biological Chemistry, vol. 283, no. 48, pp. 33175–33182, 2008. View at Publisher · View at Google Scholar · View at Scopus
  171. G. R. Campbell and S. A. Spector, “Toll-like receptor 8 ligands activate a vitamin D mediated autophagic response that inhibits human immunodeficiency virus type 1,” PLoS Pathogens, vol. 8, no. 11, Article ID e1003017, 2012. View at Google Scholar
  172. Y. S. Rajawat and I. Bossis, “Autophagy in aging and in neurodegenerative disorders,” Hormones, vol. 7, no. 1, pp. 46–61, 2008. View at Google Scholar · View at Scopus
  173. C. Lopez-Otin, M. A. Blasco, L. Partridge, M. Serrano, and G. Kroemer, “The hallmarks of aging,” Cell, vol. 153, no. 6, pp. 1194–1217, 2013. View at Publisher · View at Google Scholar
  174. F. Madeo, N. Tavernarakis, and G. Kroemer, “Can autophagy promote longevity?” Nature Cell Biology, vol. 12, no. 9, pp. 842–846, 2010. View at Publisher · View at Google Scholar · View at Scopus
  175. D. C. Rubinsztein, G. Mariño, and G. Kroemer, “Autophagy and aging,” Cell, vol. 146, no. 5, pp. 682–695, 2011. View at Publisher · View at Google Scholar · View at Scopus
  176. T. Vellai, K. Takács-Vellai, M. Sass, and D. J. Klionsky, “The regulation of aging: does autophagy underlie longevity?” Trends in Cell Biology, vol. 19, no. 10, pp. 487–494, 2009. View at Publisher · View at Google Scholar · View at Scopus
  177. L. Partridge, N. Alic, I. Bjedov, and M. D. W. Piper, “Ageing in Drosophila: the role of the insulin/Igf and TOR signalling network,” Experimental Gerontology, vol. 46, no. 5, pp. 376–381, 2011. View at Publisher · View at Google Scholar · View at Scopus
  178. M. M. Lipinski, B. Zheng, T. Lu et al., “Genome-wide analysis reveals mechanisms modulating autophagy in normal brain aging and in Alzheimer's disease,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 32, pp. 14164–14169, 2010. View at Publisher · View at Google Scholar · View at Scopus
  179. M. Shibata, T. Lu, T. Furuya et al., “Regulation of intracellular accumulation of mutant huntingtin by beclin 1,” Journal of Biological Chemistry, vol. 281, no. 20, pp. 14474–14485, 2006. View at Publisher · View at Google Scholar · View at Scopus
  180. F. Pickford, E. Masliah, M. Britschgi et al., “The autophagy-related protein beclin 1 shows reduced expression in early Alzheimer disease and regulates amyloid β accumulation in mice,” Journal of Clinical Investigation, vol. 118, no. 6, pp. 2190–2199, 2008. View at Publisher · View at Google Scholar · View at Scopus
  181. T. Hara, K. Nakamura, M. Matsui et al., “Suppression of basal autophagy in neural cells causes neurodegenerative disease in mice,” Nature, vol. 441, no. 7095, pp. 885–889, 2006. View at Publisher · View at Google Scholar · View at Scopus
  182. M. Komatsu, S. Waguri, T. Chiba et al., “Loss of autophagy in the central nervous system causes neurodegeneration in mice,” Nature, vol. 441, no. 7095, pp. 880–884, 2006. View at Publisher · View at Google Scholar · View at Scopus
  183. C. Zhang and A. M. Cuervo, “Restoration of chaperone-mediated autophagy in aging liver improves cellular maintenance and hepatic function,” Nature Medicine, vol. 14, no. 9, pp. 959–965, 2008. View at Publisher · View at Google Scholar · View at Scopus
  184. M. Taneike, O. Yamaguchi, A. Nakai et al., “Inhibition of autophagy in the heart induces age-related cardiomyopathy,” Autophagy, vol. 6, no. 5, pp. 600–606, 2010. View at Publisher · View at Google Scholar · View at Scopus
  185. S. F. Chen, M. L. Kang, Y. C. Chen et al., “Autophagy-related gene 7 is downstream of heat shock protein 27 in the regulation of eye morphology, polyglutamine toxicity, and lifespan in Drosophila,” Journal of Biomedical Science, vol. 19, article 52, 2012. View at Publisher · View at Google Scholar
  186. C. Kenyon, J. Chang, E. Gensch, A. Rudner, and R. Tabtiang, “A C. elegans mutant that lives twice as long as wild type,” Nature, vol. 366, no. 6454, pp. 461–464, 1993. View at Publisher · View at Google Scholar · View at Scopus
  187. K. Lin, J. B. Dorman, A. Rodan, and C. Kenyon, “daf-16: an HNF-3/forkhead family member that can function to double the life-span of Caenorhabditis elegans,” Science, vol. 278, no. 5341, pp. 1319–1322, 1997. View at Publisher · View at Google Scholar · View at Scopus
  188. A. Meléndez, Z. Tallóczy, M. Seaman, E.-L. Eskelinen, D. H. Hall, and B. Levine, “Autophagy genes are essential for dauer development and life-span extension in C. elegans,” Science, vol. 301, no. 5638, pp. 1387–1391, 2003. View at Publisher · View at Google Scholar · View at Scopus
  189. M. Tatar, A. Kopelman, D. Epstein, M.-P. Tu, C.-M. Yin, and R. S. Garofalo, “A mutant Drosophila insulin receptor homolog that extends life-span and impairs neuroendocrine function,” Science, vol. 292, no. 5514, pp. 107–110, 2001. View at Publisher · View at Google Scholar · View at Scopus
  190. D. J. Clancy, D. Gems, L. G. Harshman et al., “Extension of life-span by loss of CHICO, a Drosophila insulin receptor substrate protein,” Science, vol. 292, no. 5514, pp. 104–106, 2001. View at Publisher · View at Google Scholar · View at Scopus
  191. R. Yamamoto and M. Tatar, “Insulin receptor substrate chico acts with the transcription factor FOXO to extend Drosophila lifespan,” Aging Cell, vol. 10, no. 4, pp. 729–732, 2011. View at Publisher · View at Google Scholar · View at Scopus
  192. C. Slack, M. E. Giannakou, A. Foley, M. Goss, and L. Partridge, “dFOXO-independent effects of reduced insulin-like signaling in Drosophila,” Aging Cell, vol. 10, no. 5, pp. 735–748, 2011. View at Publisher · View at Google Scholar · View at Scopus
  193. D. S. Hwangbo, B. Gershman, M.-P. Tu, M. Palmer, and M. Tatar, “Drosophila dFOXO controls lifespan and regulates insulin signalling in brain and fat body,” Nature, vol. 429, no. 6991, pp. 562–566, 2004. View at Google Scholar
  194. H. Bai, P. Kang, A. M. Hernandez, and M. Tatar, “Activin signaling targeted by insulin/dFOXO regulates aging and muscle proteostasis in Drosophila,” PLoS Genetics, vol. 9, no. 11, Article ID e1003941, 2013. View at Google Scholar
  195. F. Demontis and N. Perrimon, “FOXO/4E-BP signaling in Drosophila muscles regulates organism-wide proteostasis during aging,” Cell, vol. 143, no. 5, pp. 813–825, 2010. View at Publisher · View at Google Scholar · View at Scopus
  196. M. C. Wang, D. Bohmann, and H. Jasper, “JNK signaling confers tolerance to oxidative stress and extends lifespan in Drosophila,” Developmental Cell, vol. 5, no. 5, pp. 811–816, 2003. View at Publisher · View at Google Scholar · View at Scopus
  197. M. C. Wang, D. Bohmann, and H. Jasper, “JNK extends life span and limits growth by antagonizing cellular and organism-wide responses to insulin signaling,” Cell, vol. 121, no. 1, pp. 115–125, 2005. View at Publisher · View at Google Scholar · View at Scopus
  198. H. Wu, M. C. Wang, and D. Bohmann, “JNK protects Drosophila from oxidative stress by trancriptionally activating autophagy,” Mechanisms of Development, vol. 126, no. 8-9, pp. 624–637, 2009. View at Publisher · View at Google Scholar · View at Scopus
  199. T. Eisenberg, H. Knauer, A. Schauer et al., “Induction of autophagy by spermidine promotes longevity,” Nature Cell Biology, vol. 11, no. 11, pp. 1305–1314, 2009. View at Publisher · View at Google Scholar · View at Scopus
  200. V. K. Gupta, L. Scheunemann, T. Eisenberg et al., “Restoring polyamines protects from age-induced memory impairment in an autophagy-dependent manner,” Nature Neuroscience, vol. 16, no. 10, pp. 1453–1460, 2013. View at Publisher · View at Google Scholar
  201. N. Minois, D. Carmona-Gutierrez, M. A. Bauer et al., “Spermidine promotes stress resistance in Drosophila melanogaster through autophagy-dependent and -independent pathways,” Cell Death & Disease, vol. 3, p. e401, 2012. View at Google Scholar
  202. I. Bjedov, J. M. Toivonen, F. Kerr et al., “Mechanisms of life span extension by rapamycin in the fruit fly Drosophila melanogaster,” Cell Metabolism, vol. 11, no. 1, pp. 35–46, 2010. View at Publisher · View at Google Scholar · View at Scopus
  203. P. Kapahi, B. M. Zid, T. Harper, D. Koslover, V. Sapin, and S. Benzer, “Regulation of lifespan in Drosophila by modulation of genes in the TOR signaling pathway,” Current Biology, vol. 14, no. 10, pp. 885–890, 2004. View at Publisher · View at Google Scholar · View at Scopus
  204. M. D. W. Piper and L. Partridge, “Dietary restriction in Drosophila: delayed aging or experimental artefact?” PLoS Genetics, vol. 3, no. 4, p. e57, 2007. View at Publisher · View at Google Scholar · View at Scopus
  205. K. Jia and B. Levine, “Autophagy is required for dietary restriction-mediated life span extension in C. elegans,” Autophagy, vol. 3, no. 6, pp. 597–599, 2007. View at Google Scholar · View at Scopus
  206. M. L. Tóth, T. Sigmond, É. Borsos et al., “Longevity pathways converge on autophagy genes to regulate life span in Caenorhabditis elegans,” Autophagy, vol. 4, no. 3, pp. 330–338, 2008. View at Google Scholar · View at Scopus
  207. M. Jaiswal, H. Sandoval, K. Zhang, V. Bayat, and H. J. Bellen, “Probing mechanisms that underlie human neurodegenerative diseases in Drosophila,” Annual Review of Genetics, vol. 46, pp. 371–396, 2012. View at Publisher · View at Google Scholar
  208. J. H. Son, J. H. Shim, K.-H. Kim, J.-Y. Ha, and J. Y. Han, “Neuronal autophagy and neurodegenerative diseases,” Experimental and Molecular Medicine, vol. 44, no. 2, pp. 89–98, 2012. View at Publisher · View at Google Scholar · View at Scopus
  209. G. R. Jackson, I. Salecker, X. Dong et al., “Polyglutamine-expanded human huntingtin transgenes induce degeneration of Drosophila photoreceptor neurons,” Neuron, vol. 21, no. 3, pp. 633–642, 1998. View at Publisher · View at Google Scholar · View at Scopus
  210. B. Ravikumar, C. Vacher, Z. Berger et al., “Inhibition of mTOR induces autophagy and reduces toxicity of polyglutamine expansions in fly and mouse models of Huntington disease,” Nature Genetics, vol. 36, no. 6, pp. 585–595, 2004. View at Publisher · View at Google Scholar · View at Scopus
  211. Z. Berger, B. Ravikumar, F. M. Menzies et al., “Rapamycin alleviates toxicity of different aggregate-prone proteins,” Human Molecular Genetics, vol. 15, no. 3, pp. 433–442, 2006. View at Publisher · View at Google Scholar · View at Scopus
  212. S. Sarkar, E. O. Perlstein, S. Imarisio et al., “Small molecules enhance autophagy and reduce toxicity in Huntington's disease models,” Nature Chemical Biology, vol. 3, no. 6, pp. 331–338, 2007. View at Publisher · View at Google Scholar · View at Scopus
  213. R. A. Floto, S. Sarkar, E. O. Perlstein, B. Kampmann, S. L. Schreiber, and D. C. Rubinsztein, “Small molecule enhancers of rapamycin-induced TOR inhibition promote autophagy, reduce toxicity in Huntington's disease models and enhance killing of mycobacteria by macrophages,” Autophagy, vol. 3, no. 6, pp. 620–622, 2007. View at Google Scholar · View at Scopus
  214. B. Ravikumar, S. Imarisio, S. Sarkar, C. J. O'Kane, and D. C. Rubinsztein, “Rab5 modulates aggregation and toxicity of mutant huntingtin through macroautophagy in cell and fly models of Huntington disease,” Journal of Cell Science, vol. 121, no. 10, pp. 1649–1660, 2008. View at Publisher · View at Google Scholar · View at Scopus
  215. T. Wang, U. Lao, and B. A. Edgar, “TOR-mediated autophagy regulates cell death in Drosophila neurodegenerative disease,” The Journal of Cell Biology, vol. 186, no. 5, pp. 703–711, 2009. View at Publisher · View at Google Scholar · View at Scopus
  216. F. M. Menzies, R. Hourez, S. Imarisio et al., “Puromycin-sensitive aminopeptidase protects against aggregation-prone proteins via autophagy,” Human Molecular Genetics, vol. 19, no. 23, pp. 4573–4586, 2010. View at Publisher · View at Google Scholar · View at Scopus
  217. J. Bilen and N. M. Bonini, “Genome-wide screen for modifiers of ataxin-3 neurodegeneration in Drosophila,” PLoS Genetics, vol. 3, no. 10, pp. 1950–1964, 2007. View at Publisher · View at Google Scholar · View at Scopus
  218. I. Nisoli, J. P. Chauvin, F. Napoletano et al., “Neurodegeneration by polyglutamine Atrophin is not rescued by induction of autophagy,” Cell Death and Differentiation, vol. 17, no. 10, pp. 1577–1587, 2010. View at Publisher · View at Google Scholar · View at Scopus
  219. F. Napoletano, S. Occhi, P. Calamita et al., “Polyglutamine Atrophin provokes neurodegeneration in Drosophila by repressing fat,” EMBO Journal, vol. 30, no. 5, pp. 945–958, 2011. View at Publisher · View at Google Scholar · View at Scopus
  220. P. Calamita and M. Fanto, “Slimming down fat makes neuropathic hippo: the fat/hippo tumor suppressor pathway protects adult neurons through regulation of autophagy,” Autophagy, vol. 7, no. 8, pp. 907–909, 2011. View at Publisher · View at Google Scholar · View at Scopus
  221. R. A. Nixon, J. Wegiel, A. Kumar et al., “Extensive involvement of autophagy in Alzheimer disease: an immuno-electron microscopy study,” Journal of Neuropathology and Experimental Neurology, vol. 64, no. 2, pp. 113–122, 2005. View at Google Scholar · View at Scopus
  222. D. Ling, H.-J. Song, D. Garza, T. P. Neufeld, and P. M. Salvaterra, “Abeta42-induced neurodegeneration via an age-dependent autophagic-lysosomal injury in Drosophila,” PLoS ONE, vol. 4, no. 1, Article ID e4201, 2009. View at Publisher · View at Google Scholar · View at Scopus
  223. U. B. Pandey, Y. Batlevi, E. H. Baehrecke, and J. P. Taylor, “HDAC6 at the intersection of autophagy, the ubiquitin-proteasome system and neurodegeneration,” Autophagy, vol. 3, no. 6, pp. 643–645, 2007. View at Google Scholar · View at Scopus
  224. M. Filimonenko, S. Stuffers, C. Raiborg et al., “Functional multivesicular bodies are required for autophagic clearance of protein aggregates associated with neurodegenerative disease,” The Journal of Cell Biology, vol. 179, no. 3, pp. 485–500, 2007. View at Publisher · View at Google Scholar · View at Scopus
  225. T. E. Rusten, M. Filimonenko, L. M. Rodahl, H. Stenmark, and A. Simonsen, “ESCRTing autophagic clearance of aggregating proteins,” Autophagy, vol. 4, no. 2, pp. 233–236, 2008. View at Google Scholar · View at Scopus
  226. A. B. Birgisdottir, T. Lamark, and T. Johansen, “The LIR motif—crucial for selective autophagy,” Journal of Cell Science, vol. 126, part 15, pp. 3237–3247, 2013. View at Google Scholar
  227. P. Wild, H. Farhan, D. G. McEwan et al., “Phosphorylation of the autophagy receptor optineurin restricts Salmonella growth,” Science, vol. 333, no. 6039, pp. 228–233, 2011. View at Publisher · View at Google Scholar · View at Scopus
  228. S. Jiang, C. D. Wells, and P. J. Roach, “Starch-binding domain-containing protein 1 (Stbd1) and glycogen metabolism: identification of the Atg8 family interacting motif (AIM) in Stbd1 required for interaction with GABARAPL1,” Biochemical and Biophysical Research Communications, vol. 413, no. 3, pp. 420–425, 2011. View at Publisher · View at Google Scholar · View at Scopus
  229. T. Johansen and T. Lamark, “Selective autophagy mediated by autophagic adapter proteins,” Autophagy, vol. 7, no. 3, pp. 279–296, 2011. View at Publisher · View at Google Scholar · View at Scopus
  230. J. Moscat and M. T. Diaz-Meco, “p62 at the crossroads of autophagy, apoptosis, and cancer,” Cell, vol. 137, no. 6, pp. 1001–1004, 2009. View at Publisher · View at Google Scholar · View at Scopus
  231. S. Pankiv, T. H. Clausen, T. Lamark et al., “p62/SQSTM1 binds directly to Atg8/LC3 to facilitate degradation of ubiquitinated protein aggregates by autophagy,” Journal of Biological Chemistry, vol. 282, no. 33, pp. 24131–24145, 2007. View at Publisher · View at Google Scholar · View at Scopus
  232. M. Komatsu, H. Kurokawa, S. Waguri et al., “The selective autophagy substrate p62 activates the stress responsive transcription factor Nrf2 through inactivation of Keap1,” Nature Cell Biology, vol. 12, no. 3, pp. 213–223, 2010. View at Publisher · View at Google Scholar · View at Scopus
  233. A. Jain, T. Lamark, E. Sjøttem et al., “p62/SQSTM1 is a target gene for transcription factor NRF2 and creates a positive feedback loop by inducing antioxidant response element-driven gene transcription,” Journal of Biological Chemistry, vol. 285, no. 29, pp. 22576–22591, 2010. View at Publisher · View at Google Scholar · View at Scopus
  234. G. Bjørkøy, T. Lamark, A. Brech et al., “p62/SQSTM1 forms protein aggregates degraded by autophagy and has a protective effect on huntingtin-induced cell death,” The Journal of Cell Biology, vol. 171, no. 4, pp. 603–614, 2005. View at Publisher · View at Google Scholar · View at Scopus
  235. M. Komatsu, S. Waguri, M. Koike et al., “Homeostatic levels of p62 control cytoplasmic inclusion body formation in autophagy-deficient mice,” Cell, vol. 131, no. 6, pp. 1149–1163, 2007. View at Publisher · View at Google Scholar · View at Scopus
  236. I. P. Nezis, A. Simonsen, A. P. Sagona et al., “Ref(2)P, the Drosophila melanogaster homologue of mammalian p62, is required for the formation of protein aggregates in adult brain,” The Journal of Cell Biology, vol. 180, no. 6, pp. 1065–1071, 2008. View at Publisher · View at Google Scholar · View at Scopus
  237. I. P. Nezis, “Selective autophagy in Drosophila,” International Journal of Cell Biology, vol. 2012, Article ID 146767, 9 pages, 2012. View at Publisher · View at Google Scholar
  238. I. P. Nezis and H. Stenmark, “p62 at the interface of autophagy, oxidative stress signaling, and cancer,” Antioxidants & Redox Signaling, vol. 17, no. 5, pp. 786–793, 2012. View at Google Scholar
  239. K. Hegedus, P. Nagy, Z. Gaspari, and G. Juhasz, “The putative HORMA domain protein Atg101 dimerizes and is required for starvation-induced and selective autophagy in Drosophila,” BioMed Research International, vol. 2014, Article ID 470482, 13 pages, 2014. View at Publisher · View at Google Scholar
  240. D. J. Klionsky, A. J. Meijer, and P. Codogno, “Autophagy and p70S6 kinase,” Autophagy, vol. 1, no. 1, pp. 59–61, 2005. View at Google Scholar · View at Scopus
  241. P. Kadandale and A. A. Kiger, “Role of selective autophagy in cellular remodeling: “Self-eating” into shape,” Autophagy, vol. 6, no. 8, pp. 1194–1195, 2010. View at Publisher · View at Google Scholar · View at Scopus
  242. P. Kadandale, J. D. Stender, C. K. Glass, and A. A. Kiger, “Conserved role for autophagy in Rho1-mediated cortical remodeling and blood cell recruitment,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 23, pp. 10502–10507, 2010. View at Publisher · View at Google Scholar · View at Scopus
  243. K. D. Finley, P. T. Edeen, R. C. Cumming et al., “Blue cheese mutations define a novel, conserved gene involved in progressive neural degeneration,” Journal of Neuroscience, vol. 23, no. 4, pp. 1254–1264, 2003. View at Google Scholar · View at Scopus
  244. T. H. Clausen, T. Lamark, P. Isakson et al., “p62/SQSTM1 and ALFY interact to facilitate the formation of p62 bodies/ALIS and their degradation by autophagy,” Autophagy, vol. 6, no. 3, pp. 330–344, 2010. View at Publisher · View at Google Scholar · View at Scopus
  245. A. Simonsen, H. C. G. Birkeland, D. J. Gillooly et al., “Alfy, a novel FYVE-domain-containing protein associated with protein granules and autophagic membranes,” Journal of Cell Science, vol. 117, no. 18, pp. 4239–4251, 2004. View at Publisher · View at Google Scholar · View at Scopus
  246. M. Filimonenko, P. Isakson, K. D. Finley et al., “The selective macroautophagic degradation of aggregated proteins requires the PI3P-binding protein Alfy,” Molecular Cell, vol. 38, no. 2, pp. 265–279, 2010. View at Publisher · View at Google Scholar · View at Scopus
  247. A. Simonsen, R. C. Cumming, and K. D. Finley, “Linking lysosomal trafficking defects with changes in aging and stress response in Drosophila,” Autophagy, vol. 3, no. 5, pp. 499–501, 2007. View at Google Scholar · View at Scopus
  248. A. Simonsen, R. C. Cumming, K. Lindmo et al., “Genetic modifiers of the drosophila blue cheese gene link defects in lysosomal transport with decreased life span and altered ubiquitinated-protein profiles,” Genetics, vol. 176, no. 2, pp. 1283–1297, 2007. View at Publisher · View at Google Scholar · View at Scopus
  249. V. Arndt, N. Dick, R. Tawo et al., “Chaperone-assisted selective autophagy is essential for muscle maintenance,” Current Biology, vol. 20, no. 2, pp. 143–148, 2010. View at Publisher · View at Google Scholar · View at Scopus
  250. A. C. Massey, C. Zhang, and A. M. Cuervo, “Chaperone-mediated autophagy in aging and disease,” Current Topics in Developmental Biology, vol. 73, pp. 205–235, 2006. View at Publisher · View at Google Scholar · View at Scopus
  251. R. J. Youle and D. P. Narendra, “Mechanisms of mitophagy,” Nature Reviews Molecular Cell Biology, vol. 12, no. 1, pp. 9–14, 2011. View at Publisher · View at Google Scholar · View at Scopus
  252. T. Kanki, K. Wang, Y. Cao, M. Baba, and D. J. Klionsky, “Atg32 is a mitochondrial protein that confers selectivity during mitophagy,” Developmental Cell, vol. 17, no. 1, pp. 98–109, 2009. View at Publisher · View at Google Scholar · View at Scopus
  253. I. Novak, V. Kirkin, D. G. McEwan et al., “Nix is a selective autophagy receptor for mitochondrial clearance,” EMBO Reports, vol. 11, no. 1, pp. 45–51, 2010. View at Publisher · View at Google Scholar · View at Scopus
  254. R. L. Schweers, J. Zhang, M. S. Randall et al., “NIX is required for programmed mitochondrial clearance during reticulocyte maturation,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 49, pp. 19500–19505, 2007. View at Publisher · View at Google Scholar · View at Scopus
  255. D. Narendra, A. Tanaka, D.-F. Suen, and R. J. Youle, “Parkin is recruited selectively to impaired mitochondria and promotes their autophagy,” The Journal of Cell Biology, vol. 183, no. 5, pp. 795–803, 2008. View at Publisher · View at Google Scholar · View at Scopus
  256. D. P. Narendra, S. M. Jin, A. Tanaka et al., “PINK1 is selectively stabilized on impaired mitochondria to activate Parkin,” PLoS Biology, vol. 8, no. 1, Article ID e1000298, 2010. View at Publisher · View at Google Scholar · View at Scopus
  257. S. A. Sarraf, M. Raman, V. Guarani-Pereira et al., “Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization,” Nature, vol. 496, no. 7445, pp. 372–376, 2013. View at Publisher · View at Google Scholar
  258. I. E. Clark, M. W. Dodson, C. Jiang et al., “Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin,” Nature, vol. 441, no. 7097, pp. 1162–1166, 2006. View at Publisher · View at Google Scholar · View at Scopus
  259. J. C. Greene, A. J. Whitworth, I. Kuo, L. A. Andrews, M. B. Feany, and L. J. Pallanck, “Mitochondrial pathology and apoptotic muscle degeneration in Drosophila parkin mutants,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 7, pp. 4078–4083, 2003. View at Publisher · View at Google Scholar · View at Scopus
  260. Y. Pesah, T. Pham, H. Burgess et al., “Drosophila parkin mutants have decreased mass and cell size and increased sensitivity to oxygen radical stress,” Development, vol. 131, no. 9, pp. 2183–2194, 2004. View at Publisher · View at Google Scholar · View at Scopus
  261. H. Deng, M. W. Dodson, H. Huang, and M. Guo, “The Parkinson's disease genes pink1 and parkin promote mitochondrial fission and/or inhibit fusion in Drosophila,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 38, pp. 14503–14508, 2008. View at Publisher · View at Google Scholar · View at Scopus
  262. A. C. Poole, R. E. Thomas, S. Yu, E. S. Vincow, and L. Pallanck, “The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/parkin pathway,” PLoS ONE, vol. 5, no. 4, Article ID e10054, 2010. View at Publisher · View at Google Scholar · View at Scopus
  263. E. Ziviani, R. N. Tao, and A. J. Whitworth, “Drosophila Parkin requires PINK1 for mitochondrial translocation and ubiquitinates Mitofusin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 11, pp. 5018–5023, 2010. View at Publisher · View at Google Scholar · View at Scopus
  264. E. S. Vincow, G. Merrihew, R. E. Thomas et al., “The PINK1-Parkin pathway promotes both mitophagy and selective respiratory chain turnover in vivo,” Proceedings of the National Academy of Sciences of the United States of America, vol. 110, no. 16, pp. 6400–6405, 2013. View at Publisher · View at Google Scholar
  265. D. H. Margineantu, C. B. Emerson, D. Diaz, and D. M. Hockenbery, “Hsp90 inhibition decreases mitochondrial protein turnover,” PLoS ONE, vol. 2, no. 10, Article ID e1066, 2007. View at Publisher · View at Google Scholar · View at Scopus
  266. V. Soubannier, G.-L. McLelland, R. Zunino et al., “A vesicular transport pathway shuttles cargo from mitochondria to lysosomes,” Current Biology, vol. 22, no. 2, pp. 135–141, 2012. View at Publisher · View at Google Scholar · View at Scopus
  267. M. Neuspiel, A. C. Schauss, E. Braschi et al., “Cargo-selected transport from the mitochondria to peroxisomes is mediated by vesicular carriers,” Current Biology, vol. 18, no. 2, pp. 102–108, 2008. View at Publisher · View at Google Scholar · View at Scopus
  268. E. Taillebourg, I. Gregoire, P. Viargues et al., “The deubiquitinating enzyme USP36 controls selective autophagy activation by ubiquitinated proteins,” Autophagy, vol. 8, no. 5, pp. 767–779, 2012. View at Google Scholar
  269. H. Zhang, J. P. Stallock, J. C. Ng, C. Reinhard, and T. P. Neufeld, “Regulation of cellular growth by the Drosophila target of rapamycin dTOR,” Genes and Development, vol. 14, no. 21, pp. 2712–2724, 2000. View at Publisher · View at Google Scholar · View at Scopus
  270. M. M. Lipinski, G. Hoffman, A. Ng et al., “A genome-wide siRNA screen reveals multiple mTORC1 independent signaling pathways regulating autophagy under normal nutritional conditions,” Developmental Cell, vol. 18, no. 6, pp. 1041–1052, 2010. View at Google Scholar · View at Scopus
  271. I. Kalvari, S. Tsompanis, N. C. Mulakkal et al., “iLIR: a web resource for prediction of Atg8-family interacting proteins,” Autophagy, vol. 10, no. 5, 2014. View at Google Scholar
  272. Y. Tian, J. C. Chang, E. Y. Fan, M. Flajolet, and P. Greengard, “Adaptor complex AP2/PICALM, through interaction with LC3, targets Alzheimer's APP-CTF for terminal degradation via autophagy,” Proceedings of the National Academy of Sciences of the United States of America, vol. 110, no. 42, pp. 17071–17076, 2013. View at Publisher · View at Google Scholar
  273. S. E. Samaraweera, L. V. O'Keefe, G. R. Price, D. J. Venter, and R. I. Richards, “Distinct roles for Toll and autophagy pathways in double-stranded RNA toxicity in a Drosophila model of expanded repeat neurodegenerative diseases,” Human Molecular Genetics, vol. 22, no. 14, pp. 2811–2819, 2013. View at Publisher · View at Google Scholar
  274. S. Batelli, E. Peverelli, S. Rodilossi, G. Forloni, and D. Albani, “Macroautophagy and the proteasome are differently involved in the degradation of alpha-synuclein wild type and mutated A30P in an in vitro inducible model (PC12/TetOn),” Neuroscience, vol. 195, pp. 128–137, 2011. View at Publisher · View at Google Scholar · View at Scopus