Table of Contents Author Guidelines Submit a Manuscript
Oxidative Medicine and Cellular Longevity
Volume 2013, Article ID 601587, 6 pages
http://dx.doi.org/10.1155/2013/601587
Review Article

Function and Characteristics of PINK1 in Mitochondria

Department of Environmental Health Science, Nara Women's University, Kita-Uoya Nishimachi, Nara 630-8506, Japan

Received 14 December 2012; Revised 2 February 2013; Accepted 4 February 2013

Academic Editor: Emilio Luiz Streck

Copyright © 2013 Satoru Matsuda 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. D. G. Nicholls, “Mitochondrial ion circuits,” Essays in Biochemistry, vol. 47, pp. 25–35, 2010. View at Google Scholar
  2. I. Novak, “Mitophagy: a complex mechanism of mitochondrial removal,” Antioxidants & Redox Signaling, vol. 17, no. 5, pp. 794–802, 2012. View at Google Scholar
  3. T. Calì, D. Ottolini, and M. Brini, “Mitochondrial Ca2+ and neurodegeneration,” Cell Calcium, vol. 52, no. 1, pp. 73–85, 2012. View at Google Scholar
  4. S. Gandhi and A. Y. Abramov, “Mechanism of oxidative stress in neurodegeneration,” Oxidative Medicine and Cellular Longevity, vol. 2012, Article ID 428010, 11 pages, 2012. View at Publisher · View at Google Scholar
  5. T. Nakamura and S. A. Lipton, “Redox modulation by S-nitrosylation contributes to protein misfolding, mitochondrial dynamics, and neuronal synaptic damage in neurodegenerative diseases,” Cell Death & Differentiation, vol. 18, no. 9, pp. 1478–1486, 2011. View at Google Scholar
  6. L. R. Feng and K. A. Maguire-Zeiss, “Gene therapy in parkinsons disease: rationale and current status,” CNS Drugs, vol. 24, no. 3, pp. 177–192, 2010. View at Publisher · View at Google Scholar · View at Scopus
  7. O. Corti, S. Lesage, and A. Brice, “What genetics tells us about the causes and mechanisms of Parkinson's disease,” Physiological Reviews, vol. 91, no. 4, pp. 1161–1218, 2011. View at Google Scholar
  8. E. Deas, H. Plun-Favreau, S. Gandhi et al., “PINK1 cleavage at position A103 by the mitochondrial protease PARL,” Human Molecular Genetics, vol. 20, no. 5, pp. 867–879, 2011. View at Publisher · View at Google Scholar · View at Scopus
  9. A. W. Greene, K. Grenier, M. A. Aguileta et al., “Mitochondrial processing peptidase regulates PINK1 processing, import and Parkin recruitment,” EMBO Reports, vol. 13, no. 4, pp. 378–385, 2012. View at Google Scholar
  10. J. C. Rochet, B. A. Hay, and M. Guo, “Molecular insights into Parkinson's disease,” Progress in Molecular Biology and Translational Science, vol. 107, pp. 125–188, 2012. View at Google Scholar
  11. K. R. Kumar, A. Djarmati-Westenberger, and A. Grünewald, “Genetics of Parkinson's disease,” Seminars in Neurology, vol. 31, no. 5, pp. 433–440, 2011. View at Google Scholar
  12. J. M. Taymans, C. Van Den Haute, and V. Baekelandt, “Distribution of PINK1 and LRRK2 in rat and mouse brain,” Journal of Neurochemistry, vol. 98, no. 3, pp. 951–961, 2006. View at Publisher · View at Google Scholar · View at Scopus
  13. J. G. Blackinton, A. Anvret, A. Beilina, L. Olson, M. R. Cookson, and D. Galter, “Expression of PINK1 mRNA in human and rodent brain and in Parkinson's disease,” Brain Research, vol. 1184, no. 1, pp. 10–16, 2007. View at Publisher · View at Google Scholar · View at Scopus
  14. L. Silvestri, V. Caputo, E. Bellacchio et al., “Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism,” Human Molecular Genetics, vol. 14, no. 22, pp. 3477–3492, 2005. View at Publisher · View at Google Scholar · View at Scopus
  15. M. M. K. Muqit, P. M. Abou-Sleiman, A. T. Saurin et al., “Altered cleavage and localization of PINK1 to aggresomes in thepresence of proteasomal stress,” Journal of Neurochemistry, vol. 98, no. 1, pp. 156–169, 2006. View at Publisher · View at Google Scholar · View at Scopus
  16. A. Weihofen, K. J. Thomas, B. L. Ostaszewski, M. R. Cookson, and D. J. Selkoe, “Pink1 forms a multiprotein complex with miro and milton, linking Pink1 function to mitochondrial trafficking,” Biochemistry, vol. 48, no. 9, pp. 2045–2052, 2009. View at Publisher · View at Google Scholar · View at Scopus
  17. S. M. Jin, M. Lazarou, C. Wang, L. A. Kane, D. P. Narendra, and R. J. Youle, “Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL,” Journal of Cell Biology, vol. 191, no. 5, pp. 933–942, 2010. View at Publisher · View at Google Scholar · View at Scopus
  18. A. Pilsl and K. F. Winklhofer, “Parkin, PINK1 and mitochondrial integrity: emerging concepts of mitochondrial dysfunction in Parkinson's disease,” Acta Neuropathologica, vol. 123, no. 2, pp. 173–188, 2012. View at Google Scholar
  19. J. W. Pridgeon, J. A. Olzmann, L. S. Chin, and L. Li, “PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1,” PLOS Biology, vol. 5, no. 7, article e172, 2007. View at Google Scholar
  20. H. Plun-Favreau, K. Klupsch, N. Moisoi et al., “The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1,” Nature Cell Biology, vol. 9, no. 11, pp. 1243–1252, 2007. View at Publisher · View at Google Scholar · View at Scopus
  21. E. Desideri and L. M. Martins, “Mitochondrial stress signalling: HTRA2 and Parkinson's disease,” International Journal of Cell Biology, vol. 2012, Article ID 607929, 6 pages, 2012. View at Publisher · View at Google Scholar
  22. H. Behbahani, P. F. Pavlov, B. Wiehager, T. Nishimura, B. Winblad, and M. Ankarcrona, “Association of Omi/HtrA2 with γ-secretase in mitochondria,” Neurochemistry International, vol. 57, no. 6, pp. 668–675, 2010. View at Publisher · View at Google Scholar · View at Scopus
  23. K. M. Strauss, L. M. Martins, H. Plun-Favreau et al., “Loss of function mutations in the gene encoding Omi/HtrA2 in Parkinson's disease,” Human Molecular Genetics, vol. 14, no. 15, pp. 2099–2111, 2005. View at Publisher · View at Google Scholar · View at Scopus
  24. A. Yamamoto, M. L. Cremona, and J. E. Rothman, “Autophagy-mediated clearance of huntingtin aggregates triggered by the insulin-signaling pathway,” Journal of Cell Biology, vol. 172, no. 5, pp. 719–731, 2006. View at Publisher · View at Google Scholar · View at Scopus
  25. S. Michiorri, V. Gelmetti, E. Giarda et al., “The Parkinson-associated protein PINK1 interacts with Beclin1 and promotes autophagy,” Cell Death and Differentiation, vol. 17, no. 6, pp. 962–974, 2010. View at Publisher · View at Google Scholar · View at Scopus
  26. S. Sekine, Y. Kanamaru, M. Koike et al., “Rhomboid protease PARL mediates the mitochondrial membrane potential loss-induced cleavage of PGAM5,” Journal of Biological Chemistry, vol. 287, no. 41, pp. 34635–34645, 2012. View at Google Scholar
  27. C. A. Gautier, T. Kitada, and J. Shen, “Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, no. 32, pp. 11364–11369, 2008. View at Publisher · View at Google Scholar · View at Scopus
  28. H. L. Wang, A. H. Chou, A. S. Wu et al., “PARK6 PINK1 mutants are defective in maintaining mitochondrial membrane potential and inhibiting ROS formation of substantia nigra dopaminergic neurons,” Biochimica et Biophysica Acta, vol. 1812, no. 6, pp. 674–684, 2011. View at Publisher · View at Google Scholar · View at Scopus
  29. P. R. Gardner and I. Fridovich, “Quinolinate synthetase: the oxygen-sensitive site of de novo NAD(P)+ biosynthesis,” Archives of Biochemistry and Biophysics, vol. 284, no. 1, pp. 106–111, 1991. View at Publisher · View at Google Scholar · View at Scopus
  30. P. R. Gardner, G. Costantino, C. Szabó, and A. L. Salzman, “Nitric oxide sensitivity of the aconitases,” Journal of Biological Chemistry, vol. 272, no. 40, pp. 25071–25076, 1997. View at Publisher · View at Google Scholar · View at Scopus
  31. X. Wang, D. Winter, G. Ashrafi et al., “PINK1 and Parkin target Miro for phosphorylation and degradation to arrest mitochondrial motility,” Cell, vol. 147, no. 4, pp. 893–906, 2011. View at Google Scholar
  32. H. L. Wang, A. H. Chou, T. H. Yeh et al., “PINK1 mutants associated with recessive Parkinson's disease are defective in inhibiting mitochondrial release of cytochrome c,” Neurobiology of Disease, vol. 28, no. 2, pp. 216–226, 2007. View at Google Scholar
  33. S. J. Cherra III and C. T. Chu, “Autophagy in neuroprotection and neurodegeneration: a question of balance,” Future Neurology, vol. 3, no. 3, pp. 309–323, 2008. View at Publisher · View at Google Scholar · View at Scopus
  34. S. J. Cherra III, R. K. Dagda, and C. T. Chu, “Review: autophagy and neurodegeneration: survival at a cost?” Neuropathology and Applied Neurobiology, vol. 36, no. 2, pp. 125–132, 2010. View at Publisher · View at Google Scholar · View at Scopus
  35. R. K. Dagda, S. J. Cherra, S. M. Kulich, A. Tandon, D. Park, and C. T. Chu, “Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission,” Journal of Biological Chemistry, vol. 284, no. 20, pp. 13843–13855, 2009. View at Publisher · View at Google Scholar · View at Scopus
  36. G. Shi, J. R. Lee, D. A. Grimes et al., “Functional alteration of PARL contributes to mitochondrial dysregulation in Parkinson's disease,” Human Molecular Genetics, vol. 20, no. 10, pp. 1966–1974, 2011. View at Publisher · View at Google Scholar · View at Scopus
  37. C. T. Chu, “A pivotal role for PINK1 and autophagy in mitochondrial quality control: implications for Parkinson disease,” Human Molecular Genetics, vol. 19, no. 1, pp. R28–R37, 2010. View at Publisher · View at Google Scholar · View at Scopus
  38. R. K. Dagda and C. T. Chu, “Mitochondrial quality control: insights on how Parkinson's disease related genes PINK1, parkin, and Omi/HtrA2 interact to maintain mitochondrial homeostasis,” Journal of Bioenergetics and Biomembranes, vol. 41, no. 6, pp. 473–479, 2009. View at Publisher · View at Google Scholar · View at Scopus
  39. H. Xiong, D. Wang, L. Chen et al., “Parkin, PINK1, and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation,” Journal of Clinical Investigation, vol. 119, no. 3, pp. 650–660, 2009. View at Publisher · View at Google Scholar · View at Scopus
  40. Y. Kim, J. Park, S. Kim et al., “PINK1 controls mitochondrial localization of Parkin through direct phosphorylation,” Biochemical and Biophysical Research Communications, vol. 377, no. 3, pp. 975–980, 2008. View at Publisher · View at Google Scholar · View at Scopus
  41. D. Narendra, A. Tanaka, D. F. Suen, and R. J. Youle, “Parkin is recruited selectively to impaired mitochondria and promotes their autophagy,” Journal of Cell Biology, vol. 183, no. 5, pp. 795–803, 2008. View at Google Scholar
  42. D. P. Narendra and R. J. Youle, “Targeting mitochondrial dysfunction: role for PINK1 and parkin in mitochondrial quality control,” Antioxidants and Redox Signaling, vol. 14, no. 10, pp. 1929–1938, 2011. View at Publisher · View at Google Scholar · View at Scopus
  43. A. Kathrin Lutz, N. Exner, M. E. Fett et al., “Loss of parkin or PINK1 function increases Drp1-dependent mitochondrial fragmentation,” Journal of Biological Chemistry, vol. 284, no. 34, pp. 22938–22951, 2009. View at Publisher · View at Google Scholar · View at Scopus
  44. A. Sandebring, K. J. Thomas, A. Beilina et al., “Mitochondrial alterations in PINK1 deficient cells are influenced by calcineurin-dependent dephosphorylation of dynamin-related protein 1,” PLoS ONE, vol. 4, no. 5, Article ID e5701, 2009. View at Publisher · View at Google Scholar · View at Scopus
  45. D. Narendra, J. E. Walker, and R. Youle, “Mitochondrial quality control mediated by PINK1 and Parkin: links to Parkinsonism,” Cold Spring Harbor Perspectives in Biology, vol. 4, no. 11, 2012. View at Publisher · View at Google Scholar
  46. M. E. Gegg and A. H. V. Schapira, “PINK1-parkin-dependent mitophagy involves ubiquitination of mitofusins 1 and 2: implications for Parkinson disease pathogenesis,” Autophagy, vol. 7, no. 2, pp. 243–245, 2011. View at Publisher · View at Google Scholar · View at Scopus
  47. C. Meissner, H. Lorenz, A. Weihofen, D. J. Selkoe, and M. K. Lemberg, “The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking,” Journal of Neurochemistry, vol. 117, no. 5, pp. 856–867, 2011. View at Publisher · View at Google Scholar · View at Scopus
  48. K. Okatsu, T. Oka, M. Iguchi et al., “PINK1 autophosphorylation upon membrane potential dissipation is essential for Parkin recruitment to damaged mitochondria,” Nature Communications, vol. 3, article 1016, 2012. View at Publisher · View at Google Scholar
  49. M. R. Cookson and O. Bandmann, “Parkinson's disease: insights from pathways,” Human Molecular Genetics, vol. 19, no. 1, pp. R21–R27, 2010. View at Publisher · View at Google Scholar · View at Scopus
  50. G. J. Gu, D. Wu, H. Lund et al., “Elevated MARK2-dependent phosphorylation of Tau in Alzheimer's disease, analyzed via proximity ligation,” Journal of Alzheimer's Disease, vol. 33, no. 3, pp. 699–713, 2012. View at Google Scholar
  51. D. Matenia, C. Hempp, T. Timm, A. Eikhof, and E. M. Mandelkow, “Microtubule affinity-regulating kinase 2 (MARK2) turns on phosphatase and tensin homolog (PTEN)-induced kinase 1 (PINK1) at Thr-313, a mutation site in Parkinson disease: effects on mitochondrial transport,” Journal of Biological Chemistry, vol. 287, no. 11, pp. 8174–8186, 2012. View at Google Scholar
  52. H. Plun-Favreau, K. Klupsch, N. Moisoi et al., “The mitochondrial protease HtrA2 is regulated by Parkinson's disease-associated kinase PINK1,” Nature Cell Biology, vol. 9, no. 11, pp. 1243–1252, 2007. View at Publisher · View at Google Scholar · View at Scopus
  53. H. Plun-Favreau, S. Gandhi, A. Wood-Kaczmar, E. Deas, Z. Yao, and N. W. Wood, “What have PINK1 and HtrA2 genes told us about the role of mitochondria in Parkinson's disease?” Annals of the New York Academy of Sciences, vol. 1147, pp. 30–36, 2008. View at Publisher · View at Google Scholar · View at Scopus
  54. L. S. Tain, R. B. Chowdhury, R. N. Tao et al., “Drosophila HtrA2 is dispensable for apoptosis but acts downstream of PINK1 independently from Parkin,” Cell Death and Differentiation, vol. 16, no. 8, pp. 1118–1125, 2009. View at Publisher · View at Google Scholar · View at Scopus
  55. J. Yun, J. H. Cao, M. W. Dodson et al., “Loss-of-function analysis suggests that Omi/HtrA2 is not an essential component of the pink1/parkin pathway in vivo,” Journal of Neuroscience, vol. 28, no. 53, pp. 14500–14510, 2008. View at Publisher · View at Google Scholar · View at Scopus
  56. A. J. Whitworth and L. J. Pallanck, “The PINK1/Parkin pathway: a mitochondrial quality control system?” Journal of Bioenergetics and Biomembranes, vol. 41, no. 6, pp. 499–503, 2009. View at Publisher · View at Google Scholar · View at Scopus
  57. A. J. Whitworth, J. R. Lee, V. M. W. Ho, R. Flick, R. Chowdhury, and G. A. McQuibban, “Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin,” DMM Disease Models and Mechanisms, vol. 1, no. 2-3, pp. 168–174, 2008. View at Publisher · View at Google Scholar · View at Scopus
  58. C. A. Gautier, T. Kitada, and J. Shen, “Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress,” Proceedings of the National Academy of Sciences of the United States of America, vol. 105, pp. 11364–11369, 2008. View at Google Scholar
  59. F. Billia, L. Hauck, F. Konecny, V. Rao, J. Shen, and T. W. Mak, “PTEN-inducible kinase 1 (PINK1)/Park6 is indispensable for normal heart function,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 23, pp. 9572–9577, 2011. View at Publisher · View at Google Scholar · View at Scopus
  60. W. Liu, R. Acín-Peréz, K. D. Geghman, G. Manfredi, B. Lu, and C. Li, “Pink1 regulates the oxidative phosphorylation machinery via mitochondrial fission,” Proceedings of the National Academy of Sciences of the United States of America, vol. 108, no. 31, pp. 12920–12924, 2011. View at Publisher · View at Google Scholar · View at Scopus
  61. H. Koh and J. Chung, “PINK1 as a molecular checkpoint in the maintenance of mitochondrial function and integrity,” Molecules and Cells, vol. 34, no. 1, pp. 7–13, 2012. View at Publisher · View at Google Scholar
  62. D. Santos and S. M. Cardoso, “Mitochondrial dynamics and neuronal fate in Parkinson's disease,” Mitochondrion, vol. 12, no. 4, pp. 428–437, 2012. View at Publisher · View at Google Scholar