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A Polyubiquitin Chain Reaction: Parkin Recruitment to Damaged Mitochondria

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Vyšlo v časopise: A Polyubiquitin Chain Reaction: Parkin Recruitment to Damaged Mitochondria. PLoS Genet 11(1): e32767. doi:10.1371/journal.pgen.1004952
Kategorie: Perspective
prolekare.web.journal.doi_sk: https://doi.org/10.1371/journal.pgen.1004952

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Zdroje

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5. Kane LA, Lazarou M, Fogel AI, Li Y, Yamano K, et al. (2014) PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity. J Cell Biol 205: 143–153. doi: 10.1083/jcb.201402104 24751536

6. Iguchi M, Kujuro Y, Okatsu K, Koyano F, Kosako H, et al. (2013) Parkin-catalyzed ubiquitin-ester transfer is triggered by PINK1-dependent phosphorylation. J Biol Chem 288: 22019–22032. doi: 10.1074/jbc.M113.467530 23754282

7. Kondapalli C, Kazlauskaite A, Zhang N, Woodroof HI, Campbell DG, et al. (2012) PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65. Open Biol 2: 120080. doi: 10.1098/rsob.120080 22724072

8. Shiba-Fukushima K, Imai Y, Yoshida S, Ishihama Y, Kanao T, et al. (2012) PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy. Sci Rep 2: 1002. doi: 10.1038/srep01002 23256036

9. Chaugule VK, Burchell L, Barber KR, Sidhu A, Leslie SJ, et al. (2011) Autoregulation of Parkin activity through its ubiquitin-like domain. EMBO J 30: 2853–2867. doi: 10.1038/emboj.2011.204 21694720

10. Riley BE, Lougheed JC, Callaway K, Velasquez M, Brecht E, et al. (2013) Structure and function of Parkin E3 ubiquitin ligase reveals aspects of RING and HECT ligases. Nat Commun 4: 1982. doi: 10.1038/ncomms2982 23770887

11. Spratt DE, Martinez-Torres RJ, Noh YJ, Mercier P, Manczyk N, et al. (2013) A molecular explanation for the recessive nature of parkin-linked Parkinson's disease. Nat Commun 4: 1983. doi: 10.1038/ncomms2983 23770917

12. Spratt DE, Walden H, Shaw GS (2014) RBR E3 ubiquitin ligases: new structures, new insights, new questions. Biochem J 458: 421–437. doi: 10.1042/BJ20140006 24576094

13. Trempe JF, Sauve V, Grenier K, Seirafi M, Tang MY, et al. (2013) Structure of parkin reveals mechanisms for ubiquitin ligase activation. Science 340: 1451–1455. doi: 10.1126/science.1237908 23661642

14. Wauer T, Komander D (2013) Structure of the human Parkin ligase domain in an autoinhibited state. EMBO J 32: 2099–2112. doi: 10.1038/emboj.2013.125 23727886

15. Shiba-Fukushima K, Arano T, Matsumoto G, Inoshita T, Yoshida S, et al. (2014) Phosphorylation of Mitochondrial Polyubiquitin by PINK1 Promotes Parkin Mitochondrial Tethering. PLoS Genet 10: e1004861. doi: 10.1371/journal.pgen.1004861 25474007

16. Ordureau A, Sarraf SA, Duda DM, Heo JM, Jedrychowski MP, et al. (2014) Quantitative Proteomics Reveal a Feedforward Mechanism for Mitochondrial PARKIN Translocation and Ubiquitin Chain Synthesis. Mol Cell 56: 360–375. doi: 10.1016/j.molcel.2014.09.007 25284222

17. Bingol B, Tea JS, Phu L, Reichelt M, Bakalarski CE, et al. (2014) The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy. Nature 510: 370–375. 24896179

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19. Durcan TM, Tang MY, Perusse JR, Dashti EA, Aguileta MA, et al. (2014) USP8 regulates mitophagy by removing K6-linked ubiquitin conjugates from parkin. EMBO J 33: 2473–2491. doi: 10.15252/embj.201489729 25216678

20. Imai Y, Kanao T, Sawada T, Kobayashi Y, Moriwaki Y, et al. (2010) The loss of PGAM5 suppresses the mitochondrial degeneration caused by inactivation of PINK1 in Drosophila. PLoS Genet 6: e1001229. doi: 10.1371/journal.pgen.1001229 21151955

21. Lazarou M, Narendra DP, Jin SM, Tekle E, Banerjee S, et al. (2013) PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding. J Cell Biol 200: 163–172. doi: 10.1083/jcb.201210111 23319602

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