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Parkinson’s Disease
Volume 2011 (2011), Article ID 153979, 9 pages
http://dx.doi.org/10.4061/2011/153979
Research Article

PINK1-Interacting Proteins: Proteomic Analysis of Overexpressed PINK1

Section of Clinical and Molecular Neurogenetics, Department of Neurology, University of Lübeck, Maria-Goeppert-Straße 1, 23562 Lübeck, Germany

Received 22 November 2010; Accepted 22 December 2010

Academic Editor: Charleen T. Chu

Copyright © 2011 Aleksandar Rakovic 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. J. Hardy, P. Lewis, T. Revesz, A. Lees, and C. Paisan-Ruiz, “The genetics of Parkinson's syndromes: a critical review,” Current Opinion in Genetics and Development, vol. 19, no. 3, pp. 254–265, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  2. H. Shimura, M. G. Schlossmacher, N. Hattori et al., “Ubiquitination of a new form of α-synuclein by parkin from human brain: implications for Parkinson's disease,” Science, vol. 293, no. 5528, pp. 263–269, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  3. B. Tang, H. Xiong, P. Sun et al., “Association of PINK1 and DJ-1 confers digenic inheritance of early-onset Parkinson's disease,” Human Molecular Genetics, vol. 15, no. 11, pp. 1816–1825, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  4. 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 PubMed · View at Scopus
  5. J. Park, S. B. Lee, S. Lee et al., “Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin,” Nature, vol. 441, no. 7097, pp. 1157–1161, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  6. Y. Yang, S. Gehrke, Y. Imai et al., “Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 28, pp. 10793–10798, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  7. 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 PubMed
  8. 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 PubMed · View at Scopus
  9. M. E. Gegg, J. M. Cooper, K.-Y. Chau, M. Rojo, A. H. V. Schapira, and J.-W. Taanman, “Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy,” Human Molecular Genetics, vol. 19, no. 24, pp. 4861–4870, 2010. View at Publisher · View at Google Scholar · View at PubMed
  10. C. Klein and M. G. Schlossmacher, “Parkinson disease, 10 years after its genetic revolution: multiple clues to a complex disorder,” Neurology, vol. 69, no. 22, pp. 2093–2104, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  11. S. A. Miller, D. D. Dykes, and H. F. Polesky, “A simple salting out procedure for extracting DNA from human nucleated cells,” Nucleic Acids Research, vol. 16, no. 3, p. 1215, 1988. View at Google Scholar · View at Scopus
  12. K. Hedrich, J. Hagenah, A. Djarmati et al., “Clinical spectrum of homozygous and heterozygous PINK1 mutations in a large german family with parkinson disease: role of a single hit?” Archives of Neurology, vol. 63, no. 6, pp. 833–838, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  13. E. Moro, J. Volkmann, I. R. König et al., “Bilateral subthalamic stimulation in Parkin and PINK1 parkinsonism,” Neurology, vol. 70, no. 14, pp. 1186–1191, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  14. M. Sena-Esteves, J. C. Tebbets, S. Steffens, T. Crombleholme, and A. W. Flake, “Optimized large-scale production of high titer lentivirus vector pseudotypes,” Journal of Virological Methods, vol. 122, no. 2, pp. 131–139, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  15. E. Mortz, T. N. Krogh, H. Vorum, and A. Görg, “Improved silver staining protocols for high sensitivity protein identification using matrix-assisted laser desorption/ionization-time of flight analysis,” Proteomics, vol. 1, no. 11, pp. 1359–1363, 2001. View at Google Scholar · View at Scopus
  16. I. Topisirovic, N. Siddiqui, V. L. Lapointe et al., “Molecular dissection of the eukaryotic initiation factor 4E (eIF4E) export-competent RNP,” EMBO Journal, vol. 28, no. 8, pp. 1087–1098, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  17. A. Rakovic, A. Grünewald, P. Seibler et al., “Effect of endogenous mutant and wild-type PINK1 on Parkin in fibroblasts from Parkinson disease patients,” Human Molecular Genetics, vol. 19, no. 16, pp. 3124–3137, 2010. View at Publisher · View at Google Scholar · View at PubMed
  18. S. Mili and S. Piñol-Roma, “LRP130, a pentatricopeptide motif protein with a noncanonical RNA-binding domain, Is bound in vivo to mitochondrial and nuclear RNAs,” Molecular and Cellular Biology, vol. 23, no. 14, pp. 4972–4982, 2003. View at Publisher · View at Google Scholar · View at Scopus
  19. A. Weihofen, B. Ostaszewski, Y. Minami, and D. J. Selkoe, “Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1,” Human Molecular Genetics, vol. 17, no. 4, pp. 602–616, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  20. E. M. Valente, S. Michiorri, G. Arena, and V. Gelmetti, “PINK1: one protein, multiple neuroprotective functions,” Future Neurology, vol. 4, no. 5, pp. 575–590, 2009. View at Publisher · View at Google Scholar · View at Scopus
  21. A. J. Caplan, A. K. Mandal, and M. A. Theodoraki, “Molecular chaperones and protein kinase quality control,” Trends in Cell Biology, vol. 17, no. 2, pp. 87–92, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  22. 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 PubMed
  23. L. A. Mizzen, C. Chang, J. I. Garrels, and W. J. Welch, “Identification, characterization, and purification of two mammalian stres proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein,” Journal of Biological Chemistry, vol. 264, no. 34, pp. 20664–20675, 1989. View at Google Scholar · View at Scopus
  24. J. N. Dahlseid, R. Lill, J. M. Green, X. Xu, Y. Qiu, and S. K. Pierce, “PBP74, a new member of the mammalian 70-kDa heat shock protein family, is a mitochondrial protein,” Molecular Biology of the Cell, vol. 5, no. 11, pp. 1265–1275, 1994. View at Google Scholar · View at Scopus
  25. G. Szabadkai, K. Bianchi, P. Várnai et al., “Chaperone-mediated coupling of endoplasmic reticulum and mitochondrial Ca channels,” Journal of Cell Biology, vol. 175, no. 6, pp. 901–911, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  26. Q. Ran, R. Wadhwa, R. Kawai et al., “Extramitochondrial localization of mortalin/mthsp70/PBP74/GRP75,” Biochemical and Biophysical Research Communications, vol. 275, no. 1, pp. 174–179, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  27. E. J. Davison, K. Pennington, C. C. Hung et al., “Proteomic analysis of increased Parkin expression and its interactants provides evidence for a role in modulation of mitochondrial function,” Proteomics, vol. 9, no. 18, pp. 4284–4297, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  28. E. A. Craig, J. Kramer, and J. Kosic-Smithers, “SSC1, a member of the 70-kDa heat shock protein multigene family of Saccharomyces cerevisiae, is essential for growth,” Proceedings of the National Academy of Sciences of the United States of America, vol. 84, no. 12, pp. 4156–4160, 1987. View at Google Scholar · View at Scopus
  29. W. Voos and K. Röttgers, “Molecular chaperones as essential mediators of mitochondrial biogenesis,” Biochimica et Biophysica Acta, vol. 1592, no. 1, pp. 51–62, 2002. View at Publisher · View at Google Scholar · View at Scopus
  30. P. D'Silva, Q. Liu, W. Walter, and E. A. Craig, “Regulated interactions of mtHsp70 with Tim44 at the translocon in the mitochondrial inner membrane,” Nature Structural and Molecular Biology, vol. 11, no. 11, pp. 1084–1091, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  31. H. M. Li, T. Niki, T. Taira, S. M. M. Iguchi-Ariga, and H. Ariga, “Association of DJ-1 with chaperones and enhanced association and colocalization with mitochondrial Hsp70 by oxidative stress,” Free Radical Research, vol. 39, no. 10, pp. 1091–1099, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  32. J. Jin, G. J. Li, J. Davis et al., “Identification of novel proteins associated with both α-synuclein and DJ-1,” Molecular and Cellular Proteomics, vol. 6, no. 5, pp. 845–859, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  33. C. C. Deocaris, S. Takano, D. Priyandoko et al., “Glycerol stimulates innate chaperoning, proteasomal and stress-resistance functions: implications for geronto-manipulation,” Biogerontology, vol. 9, no. 4, pp. 269–282, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  34. B. S. Park, Y. S. Song, S. B. Yee et al., “Phospho-ser 15-p53 translocates into mitochondria and interacts with Bcl-2 and Bcl-xL in eugenol-induced apoptosis,” Apoptosis, vol. 10, no. 1, pp. 193–200, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  35. L. De Mena, E. Coto, E. Sánchez-Ferrero et al., “Mutational screening of the mortalin gene (HSPA9) in Parkinson's disease,” Journal of Neural Transmission, vol. 116, no. 10, pp. 1289–1293, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  36. J. Jin, C. Hulette, Y. Wang et al., “Proteomic identification of a stress protein, mortalin/mthsp70/GRP75: relevance to Parkinson disease,” Molecular and Cellular Proteomics, vol. 5, no. 7, pp. 1193–1204, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  37. H. Koll, B. Guiard, J. Rassow et al., “Antifolding activity of hsp60 couples protein import into the mitochondrial matrix with export to the intermembrane space,” Cell, vol. 68, no. 6, pp. 1163–1175, 1992. View at Publisher · View at Google Scholar · View at Scopus
  38. M. Y. Cheng, F. U. Hartl, J. Martin et al., “Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria,” Nature, vol. 337, no. 6208, pp. 620–625, 1989. View at Google Scholar · View at Scopus
  39. V. Veereshwarayya, P. Kumar, K. M. Rosen, R. Mestril, and H. W. Querfurth, “Differential effects of mitochondrial heat shock protein 60 and related molecular chaperones to prevent intracellular β-amyloid-induced inhibition of complex IV and limit apoptosis,” Journal of Biological Chemistry, vol. 281, no. 40, pp. 29468–29478, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  40. R. Benecke, P. Strumper, and H. Weiss, “Electron transfer complexes I and IV of platelets are abnormal in Parkinson's disease but normal in Parkinson-plus syndromes,” Brain, vol. 116, no. 6, pp. 1451–1463, 1993. View at Google Scholar · View at Scopus
  41. A. H. V. Schapira, “Evidence for mitochondrial dysfunction in Parkinson's disease—a critical appraisal,” Movement Disorders, vol. 9, no. 2, pp. 125–138, 1994. View at Google Scholar · View at Scopus
  42. V. K. Mootha, P. Lepage, K. Miller et al., “Identification of a gene causing human cytochrome c oxidase deficiency by integrative genomics,” Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 2, pp. 605–610, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  43. F. Xu, C. Morin, G. Mitchell, C. Ackerley, and B. H. Robinson, “The role of the LRPPRC (leucine-rich pentatricopeptide repeal cassette) gene in cytochrome oxidase assembly: mutation causes lowered levels of COX (cytochrome c oxidase) I and COX III mRNA,” Biochemical Journal, vol. 382, part 1, pp. 331–336, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  44. F. Sasarman, C. Brunel-Guitton, H. Antonicka et al., “LRPPRC and SLIRP interact in a ribonucleoprotein complex that regulates posttranscriptional gene expression in mitochondria,” Molecular Biology of the Cell, vol. 21, no. 8, pp. 1315–1323, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  45. N. Sondheimer, J.-K. Fang, E. Polyak, M. J. Falk, and N. G. Avadhani, “Leucine-rich pentatricopeptide-repeat containing protein regulates mitochondrial transcription,” Biochemistry, vol. 49, no. 35, pp. 7467–7473, 2010. View at Publisher · View at Google Scholar · View at PubMed
  46. M. P. Cooper, L. Qu, L. M. Rohas et al., “Defects in energy homeostasis in Leigh syndrome French Canadian variant through PGC-1α/LRP130 complex,” Genes and Development, vol. 20, no. 21, pp. 2996–3009, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  47. M. Ling, F. Merante, H. S. Chen, C. Duff, A. M. V. Duncan, and B. H. Robinson, “The human mitochondrial elongation factor tu (EF-Tu) gene: CDNA sequence, genomic localization, genomic structure, and identification of a pseudogene,” Gene, vol. 197, no. 1-2, pp. 325–336, 1997. View at Publisher · View at Google Scholar · View at Scopus
  48. S. M. Chuang, LI. Chen, D. Lambertson, M. Anand, T. G. Kinzy, and K. Madura, “Proteasome-mediated degradation of cotranslationally damaged proteins involves translation elongation factor 1A,” Molecular and Cellular Biology, vol. 25, no. 1, pp. 403–413, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  49. N. Shiina, Y. Gotoh, N. Kubomura, A. Iwamatsu, and E. Nishida, “Microtubule severing by elongation factor 1α,” Science, vol. 266, no. 5183, pp. 282–285, 1994. View at Google Scholar · View at Scopus
  50. S. R. Gross and T. G. Kinzy, “Translation elongation factor 1A is essential for regulation of the actin cytoskeleton and cell morphology,” Nature Structural and Molecular Biology, vol. 12, no. 9, pp. 772–778, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  51. T. Tong, J. Ji, S. Jin et al., “Gadd45a expression induces bim dissociation from the cytoskeleton and translocation to mitochondria,” Molecular and Cellular Biology, vol. 25, no. 11, pp. 4488–4500, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  52. L. Valente, V. Tiranti, R. M. Marsano et al., “Infantile encephalopathy and defective mitochondrial DNA translation in patients with mutations of mitochondrial elongation factors EFG1 and EFTu,” American Journal of Human Genetics, vol. 80, no. 1, pp. 44–58, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  53. F. Gillardon, “Interaction of elongation factor 1-alpha with leucine-rich repeat kinase 2 impairs kinase activity and microtubule bundling in vitro,” Neuroscience, vol. 163, no. 2, pp. 533–539, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus