References
- Deas E, Wood NW, Plun-Favreau H. Mitophagy and Parkinson's disease: the PINK1-parkin link. Biochim Biophys Acta [Internet] 2011 [cited 2014 Apr 29]; 1813:623–33. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3925795&tool=pmcentrez&rendertype=abstract; http://dx.doi.org/10.1016/j.bbamcr.2010.08.007
- Swerdlow R, Burns J, Khan S. The Alzheimer's disease mitochondrial cascade hypothesis. J Alzheimers Dis 2012; 20:265-79.
- Berman S, Pineda F, Hardwick J. Mitochondrial fission and fusion dynamics: the long and short of it. Cell Death Differ 2008; 15:1147–52; PMID:18437161; http://dx.doi.org/10.1038/cdd.2008.57
- Novak I. Mitophagy: a complex mechanism of mitochondrial removal. Antioxid Redox Signal [Internet] 2012 [cited 2012 Mar 23]; 0. Available from: http://www.ncbi.nlm.nih.gov/pubmed/22077334
- Youle RJ, Narendra DP. Mechanisms of mitophagy. Nat Rev Mol Cell Biol [Internet] 2011 [cited 2010 Dec 22]; 12:9–14. Available from: http://www.nature.com/doifinder/10.1038/nrm3028; http://dx.doi.org/10.1038/nrm3028
- Zheng X, Hunter T. Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism. Cell Res [Internet] 2013 [cited 2013 May 21]:1–12. Available from: http://www.ncbi.nlm.nih.gov/pubmed/23670163
- Geisler S, Holmström KM, Skujat D, Fiesel FC, Rothfuss OC, Kahle PJ. PINK1 / Parkin-mediated mitophagy is dependent on VDAC1 and p62 / SQSTM1. Nat Cell Biol [Internet] 2010; 12:119–31. Available from: http://dx.doi.org/10.1038/ncb2012
- Narendra DP, Jin SM, Tanaka A, Suen D-F, Gautier CA, Shen J, Cookson MR, Youle RJ. PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol [Internet] 2010; 8:e1000298. Available from: http://www.ncbi.nlm.nih.gov/pubmed/20126261; http://dx.doi.org/10.1371/journal.pbio.1000298
- Narendra D, Tanaka A, Suen D-F, Youle RJ. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol [Internet] 2008; 183:795–803. Available from: http://www.ncbi.nlm.nih.gov/pubmed/19029340; http://dx.doi.org/10.1083/jcb.200809125
- Chan NC, Salazar AM, Pham AH, Sweredoski MJ, Kolawa NJ, Graham RLJ, Hess S, Chan DC. Broad activation of the ubiquitin-proteasome system by Parkin is critical for mitophagy. Hum Mol Genet [Internet] 2011 [cited 2011 Feb 10]:1–12. Available from: http://www.ncbi.nlm.nih.gov/pubmed/21296869
- Okatsu K, Saisho K, Shimanuki M, Nakada K, Shitara H, Sou Y-S, Kimura M, Sato S, Hattori N, Komatsu M, et al. p62/SQSTM1 cooperates with Parkin for perinuclear clustering of depolarized mitochondria. Genes Cells [Internet] 2010 [cited 2010 Aug 16]; 15:887–900. Available from: http://www.ncbi.nlm.nih.gov/pubmed/20604804
- Olzmann JA, Li L, Chudaev MV, Chen J, Perez FA, Palmiter RD, Chin LS. Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6. J Cell Biol [Internet] 2007 [cited 2014 Apr 29]; 178:1025–38. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2064625&tool=pmcentrez&rendertype=abstract; http://dx.doi.org/10.1083/jcb.200611128
- Johansen T, Lamark T. Selective autophagy mediated by autophagic adapter proteins. Autophagy [Internet] 2011 [cited 2014 May 24]; 7:279–96. Available from: http://www.landesbioscience.com/journals/autophagy/article/14487/; http://dx.doi.org/10.4161/auto.7.3.14487
- Kim I, Rodriguez-Enriquez S, Lemasters JJ. Selective degradation of mitochondria by mitophagy. Arch Biochem Biophys [Internet] 2007 [cited 2010 Nov 19]; 462:245–53. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=2756107&tool=pmcentrez&rendertype=abstract; http://dx.doi.org/10.1016/j.abb.2007.03.034
- Kondapalli C, Kazlauskaite A, Zhang N, Woodroof HI, Campbell DG, Gourlay R, Burchell L, Walden H, Macartney TJ, Deak M, et al. PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65. Open Biol [Internet] 2012 [cited 2012 Dec 2]; 2:120080. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3376738&tool=pmcentrez&rendertype=abstract; http://dx.doi.org/10.1098/rsob.120080
- Kane LA, Lazarou M, Fogel AI, Li Y, Yamano K, Sarraf SA, Banerjee S, Youle RJ. PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity. J Cell Biol [Internet] 2014 [cited 2014 Apr 28]; Available from: http://www.ncbi.nlm.nih.gov/pubmed/24751536
- Chen Y, Dorn Ii GW. PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria. Science (80- ) 2013; 340:471–5; http://dx.doi.org/10.1126/science.1231031
- Kazlauskaite A, Kondapalli C, Gourlay R, Campbell DG, Ritorto MS, Hofmann K, Alessi DR, Knebel A, Trost M, Muqit MMK. Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at Ser65. Biochem J [Internet] 2014 [cited 2014 Jun 2]; 460:127–39. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=4000136&tool=pmcentrez&rendertype=abstract; http://dx.doi.org/10.1042/BJ20140334
- Reyes-Turcu FE, Ventii KH, Wilkinson KD. Regulation and cellular roles of ubiquitin-specific deubiquitinating enzymes. Annu Rev Biochem [Internet] 2009; 78:363–97. Available from: http://www.ncbi.nlm.nih.gov/pubmed/19489724; http://dx.doi.org/10.1146/annurev.biochem.78.082307.091526
- Sciences B. Regulation of mitochondrial morphology by USP30, a deubiquitinating enzyme present in the mitochondrial outer membrane nobuhiro nakamura and shigehisa hirose. 2008; 19:1903–11
- Deosaran E, Larsen KB, Hua R, Sargent G, Wang Y, Kim S, Lamark T, Jauregui M, Law K, Lippincott-Schwartz J, et al. NBR1 acts as an autophagy receptor for peroxisomes. J Cell Sci [Internet] 2013 [cited 2014 Jun 5]; 126:939–52. Available from: http://www.ncbi.nlm.nih.gov/pubmed/23239026; http://dx.doi.org/10.1242/jcs.114819
- Wang Y, Nartiss Y, Steipe B, McQuibban GA, Kim PK. ROS-induced mitochondrial depolarization initiates PARK2/PARKIN-dependent mitochondrial degradation by autophagy. Autophagy [Internet] 2012; 8:1462–76. Available from: http://www.ncbi.nlm.nih.gov/pubmed/22889933; http://dx.doi.org/10.4161/auto.21211
- Eletr ZM, Wilkinson KD. Regulation of proteolysis by human deubiquitinating enzymes. Biochim Biophys Acta [Internet] 2014 [cited 2014 Apr 29]; 1843:114–28. Available from: http://www.ncbi.nlm.nih.gov/pubmed/23845989; http://dx.doi.org/10.1016/j.bbamcr.2013.06.027
- Durcan TM, Tang MY, Pérusse JR, Dashti EA, Aguileta MA, Mclelland L, Gros P, Shaler TA, Faubert D, Coulombe B, et al. USP 8 regulates mitophagy by removing K 6 -linked ubiquitin conjugates from parkin. EMBO J 2014; 33:2473–91; PMID:25216678; http://dx.doi.org/10.15252/embj.201489729
- Cornelissen T, Haddad D, Wauters F, Van Humbeeck C, Mandemakers W, Koentjoro B, Sue C, Gevaert K, De Strooper B, Verstreken P, et al. The deubiquitinase USP15 antagonizes Parkin-mediated mitochondrial ubiquitination and mitophagy. Hum Mol Genet [Internet] 2014 [cited 2014 Nov 25]; 23:5227–42. Available from: http://www.ncbi.nlm.nih.gov/pubmed/24852371; http://dx.doi.org/10.1093/hmg/ddu244
- Bingol B, Tea JS, Phu L, Reichelt M, Bakalarski CE, Song Q, Foreman O, Kirkpatrick DS, Sheng M. The mitochondrial deubiquitinase USP30 opposes parkin-mediated mitophagy. Nature [Internet] 2014 [cited 2014 Jun 4]; Available from: http://www.nature.com/doifinder/10.1038/nature13418
- Yue W, Chen Z, Liu H, Yan C, Chen M, Feng D, Yan C, Wu H, Du L, Wang Y, et al. A small natural molecule promotes mitochondrial fusion through inhibition of the deubiquitinase USP30. Cell Res 2014; 24:482–96; PMID:24513856; http://dx.doi.org/10.1038/cr.2014.20
- Xie R, Nguyen S, McKeehan K, Wang F, McKeehan WL, Liu L. Microtubule-associated protein 1S (MAP1S) bridges autophagic components with microtubules and mitochondria to affect autophagosomal biogenesis and degradation. J Biol Chem [Internet] 2011 [cited 2014 Apr 29]; 286:10367–77. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3060490&tool=pmcentrez&rendertype=abstract; http://dx.doi.org/10.1074/jbc.M110.206532
- Rambold AS, Kostelecky B, Elia N, Lippincott-schwartz J. Tubular network formation protects mitochondria from autophagosomal degradation during nutrient starvation. PNAS 2011; 108:10190–5; PMID:21646527; http://dx.doi.org/10.1073/pnas.1107402108
- Gomes LC, Di Benedetto G, Scorrano L, Di Benedetto G. During autophagy mitochondria elongate, are spared from degradation and sustain cell viability. Nat Cell Biol [Internet] 2011 [cited 2011 Apr 13]; 13:589–98. Available from: http://www.ncbi.nlm.nih.gov/pubmed/21478857; http://dx.doi.org/10.1038/ncb2220
- Youle RJ, van der Bliek AM. Mitochondrial fission, fusion, and stress. Science [Internet] 2012 [cited 2014 May 25]; 337:1062–5. Available from: http://www.ncbi.nlm.nih.gov/pubmed/22936770; http://dx.doi.org/10.1126/science.1219855
- Nunnari J, Suomalainen A. Mitochondria: in sickness and in health. Cell [Internet] 2012 [cited 2014 Apr 29]; 148:1145–59. Available from: http://www.ncbi.nlm.nih.gov/pubmed/22424226; http://dx.doi.org/10.1016/j.cell.2012.02.035
- Wunder C, Lippincott-Schwartz J, Lorenz H. Determining membrane protein topologies in single cells and high-throughput screening applications. Curr Protoc cell Biol [Internet] 2010 [cited 2014 Dec 5]; Chapter 5:Unit 5.7. Available from: http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=3018527&tool=pmcentrez&rendertype=abstract