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Volumn 6, Issue 7, 2010, Pages 871-878

The PINK1/Parkin-mediated mitophagy is compromised by PD-associated mutations

Author keywords

Autophagy; Mitochondria; Mitophagy; p62 SQSTM1; Parkin; Parkinson disease; PINK1; Ubiquitin; VDAC1

Indexed keywords

PARKIN; PINK1 ENZYME; PROTEIN SERINE THREONINE KINASE; UNCLASSIFIED DRUG;

EID: 77957673363     PISSN: 15548627     EISSN: 15548635     Source Type: Journal    
DOI: 10.4161/auto.6.7.13286     Document Type: Article
Times cited : (250)

References (30)
  • 1
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • Lin MT, Beal MF. Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 2006; 443:787-95.
    • (2006) Nature , vol.443 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 2
    • 56049091236 scopus 로고    scopus 로고
    • PINK1 controls mitochondrial localization of Parkin through direct phosphorylation
    • Kim Y, Park J, Kim S, Song S, Kwon SK, Lee SH, et al. PINK1 controls mitochondrial localization of Parkin through direct phosphorylation. Biochem Biophys Res Commun 2008; 377:975-80.
    • (2008) Biochem Biophys Res Commun , vol.377 , pp. 975-980
    • Kim, Y.1    Park, J.2    Kim, S.3    Song, S.4    Kwon, S.K.5    Lee, S.H.6
  • 3
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra D, Tanaka A, Suen DF, Youle RJ. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J Cell Biol 2008; 183:795-803.
    • (2008) J Cell Biol , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 5
    • 77950371695 scopus 로고    scopus 로고
    • PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy
    • Kawajiri S, Saiki S, Sato S, Sato F, Hatano T, Eguchi H, et al. PINK1 is recruited to mitochondria with parkin and associates with LC3 in mitophagy. FEBS Lett 2010; 584:1073-9.
    • (2010) FEBS Lett , vol.584 , pp. 1073-1079
    • Kawajiri, S.1    Saiki, S.2    Sato, S.3    Sato, F.4    Hatano, T.5    Eguchi, H.6
  • 6
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • Matsuda N, Sato S, Shiba K, Okatsu K, Saisho K, Gautier CA, et al. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J Cell Biol 2010; 189:211-21.
    • (2010) J Cell Biol , vol.189 , pp. 211-221
    • Matsuda, N.1    Sato, S.2    Shiba, K.3    Okatsu, K.4    Saisho, K.5    Gautier, C.A.6
  • 7
    • 75749156257 scopus 로고    scopus 로고
    • PINK1 is selectively stabilized on impaired mitochondria to activate Parkin
    • Narendra DP, Jin SM, Tanaka A, Suen DF, Gautier CA, Shen J, et al. PINK1 is selectively stabilized on impaired mitochondria to activate Parkin. PLoS Biol 2010; 8:1000298.
    • (2010) PLoS Biol , vol.8 , pp. 1000298
    • Narendra, D.P.1    Jin, S.M.2    Tanaka, A.3    Suen, D.F.4    Gautier, C.A.5    Shen, J.6
  • 8
    • 77955029885 scopus 로고    scopus 로고
    • Effect of endogenous mutant and wild-type PINK1 on Parkin in fibroblasts from Parkinson disease patients
    • Rakovic A, Grunewald A, Seibler P, Ramirez A, Kock N, Orolicki S, et al. Effect of endogenous mutant and wild-type PINK1 on Parkin in fibroblasts from Parkinson disease patients. Hum Mol Genet 2010; 19:3124-37.
    • (2010) Hum Mol Genet , vol.19 , pp. 3124-3137
    • Rakovic, A.1    Grunewald, A.2    Seibler, P.3    Ramirez, A.4    Kock, N.5    Orolicki, S.6
  • 10
    • 33644543761 scopus 로고    scopus 로고
    • Expanding insights of mitochondrial dysfunction in Parkinson disease
    • Abou-Sleiman PM, Muqit MM, Wood NW. Expanding insights of mitochondrial dysfunction in Parkinson disease. Nat Rev Neurosci 2006; 7:207-19.
    • (2006) Nat Rev Neurosci , vol.7 , pp. 207-219
    • Abou-Sleiman, P.M.1    Muqit, M.M.2    Wood, N.W.3
  • 11
    • 45249112594 scopus 로고    scopus 로고
    • Characterization of PINK1 processing, stability and subcellular localization
    • Lin W, Kang UJ. Characterization of PINK1 processing, stability and subcellular localization. J Neurochem 2008; 106:464-74.
    • (2008) J Neurochem , vol.106 , pp. 464-474
    • Lin, W.1    Kang, U.J.2
  • 13
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark IE, Dodson MW, Jiang C, Cao JH, Huh JR, Seol JH, et al. Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature 2006; 441:1162-6.
    • (2006) Nature , vol.441 , pp. 1162-1166
    • Clark, I.E.1    Dodson, M.W.2    Jiang, C.3    Cao, J.H.4    Huh, J.R.5    Seol, J.H.6
  • 14
    • 36049038504 scopus 로고    scopus 로고
    • Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin
    • Exner N, Treske B, Paquet D, Holmstrom K, Schiesling C, Gispert S, et al. Loss-of-function of human PINK1 results in mitochondrial pathology and can be rescued by parkin. J Neurosci 2007; 27:12413-8.
    • (2007) J Neurosci , vol.27 , pp. 12413-12418
    • Exner, N.1    Treske, B.2    Paquet, D.3    Holmstrom, K.4    Schiesling, C.5    Gispert, S.6
  • 15
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park J, Lee SB, Lee S, Kim Y, Song S, Kim S, et al. Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature 2006; 441:1157-61.
    • (2006) Nature , vol.441 , pp. 1157-1161
    • Park, J.1    Lee, S.B.2    Lee, S.3    Kim, Y.4    Song, S.5    Kim, S.6
  • 19
    • 65649118917 scopus 로고    scopus 로고
    • Parkin, PINK1 and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation
    • Xiong H, Wang D, Chen L, Choo YS, Ma H, Tang C, et al. Parkin, PINK1 and DJ-1 form a ubiquitin E3 ligase complex promoting unfolded protein degradation. J Clin Invest 2009; 119:650-60.
    • (2009) J Clin Invest , vol.119 , pp. 650-660
    • Xiong, H.1    Wang, D.2    Chen, L.3    Choo, Y.S.4    Ma, H.5    Tang, C.6
  • 20
    • 77949478474 scopus 로고    scopus 로고
    • Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NFkappaB signaling
    • Sha D, Chin LS, Li L. Phosphorylation of parkin by Parkinson disease-linked kinase PINK1 activates parkin E3 ligase function and NFkappaB signaling. Hum Mol Genet 2010; 19:352-63.
    • (2010) Hum Mol Genet , vol.19 , pp. 352-363
    • Sha, D.1    Chin, L.S.2    Li, L.3
  • 21
    • 44449099088 scopus 로고    scopus 로고
    • Clinical and molecular characterisation of a Parkinson family with a novel PINK1 mutation
    • Prestel J, Gempel K, Hauser TK, Schweitzer K, Prokisch H, Ahting U, et al. Clinical and molecular characterisation of a Parkinson family with a novel PINK1 mutation. J Neurol 2008; 255:643-8.
    • (2008) J Neurol , vol.255 , pp. 643-648
    • Prestel, J.1    Gempel, K.2    Hauser, T.K.3    Schweitzer, K.4    Prokisch, H.5    Ahting, U.6
  • 24
    • 17644365438 scopus 로고    scopus 로고
    • Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
    • Beilina A, Van Der Brug M, Ahmad R, Kesavapany S, Miller DW, Petsko GA, et al. Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc Natl Acad Sci USA 2005; 102:5703-8.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 5703-5708
    • Beilina, A.1    Van Der Brug, M.2    Ahmad, R.3    Kesavapany, S.4    Miller, D.W.5    Petsko, G.A.6
  • 25
    • 38849155699 scopus 로고    scopus 로고
    • Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1
    • Weihofen A, Ostaszewski B, Minami Y, Selkoe DJ. Pink1 Parkinson mutations, the Cdc37/Hsp90 chaperones and Parkin all influence the maturation or subcellular distribution of Pink1. Hum Mol Genet 2008; 17:602-16.
    • (2008) Hum Mol Genet , vol.17 , pp. 602-616
    • Weihofen, A.1    Ostaszewski, B.2    Minami, Y.3    Selkoe, D.J.4
  • 26
    • 33745068109 scopus 로고    scopus 로고
    • Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress
    • Muqit MM, Abou-Sleiman PM, Saurin AT, Harvey K, Gandhi S, Deas E, et al. Altered cleavage and localization of PINK1 to aggresomes in the presence of proteasomal stress. J Neurochem 2006; 98:156-69.
    • (2006) J Neurochem , vol.98 , pp. 156-169
    • Muqit, M.M.1    Abou-Sleiman, P.M.2    Saurin, A.T.3    Harvey, K.4    Gandhi, S.5    Deas, E.6
  • 27
    • 27944444154 scopus 로고    scopus 로고
    • Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism
    • Silvestri L, Caputo V, Bellacchio E, Atorino L, Dallapiccola B, Valente EM, et al. Mitochondrial import and enzymatic activity of PINK1 mutants associated to recessive parkinsonism. Hum Mol Genet 2005; 14:3477-92.
    • (2005) Hum Mol Genet , vol.14 , pp. 3477-3492
    • Silvestri, L.1    Caputo, V.2    Bellacchio, E.3    Atorino, L.4    Dallapiccola, B.5    Valente, E.M.6
  • 28
    • 34547127902 scopus 로고    scopus 로고
    • PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1
    • Pridgeon JW, Olzmann JA, Chin LS, Li L. PINK1 protects against oxidative stress by phosphorylating mitochondrial chaperone TRAP1. PLoS Biol 2007; 5:172.
    • (2007) PLoS Biol , vol.5 , pp. 172
    • Pridgeon, J.W.1    Olzmann, J.A.2    Chin, L.S.3    Li, L.4
  • 29
    • 67649399288 scopus 로고    scopus 로고
    • Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission
    • Dagda RK, Cherra SJ, 3rd, Kulich SM, Tandon A, Park D, Chu CT. Loss of PINK1 function promotes mitophagy through effects on oxidative stress and mitochondrial fission. J Biol Chem 2009; 284:13843-55.
    • (2009) J Biol Chem , vol.284 , pp. 13843-13855
    • Dagda, R.K.1    Cherra III, S.J.2    Kulich, S.M.3    Tandon, A.4    Park, D.5    Chu, C.T.6
  • 30
    • 0041935939 scopus 로고    scopus 로고
    • US National Institute of Health, Bethesda, Maryland, USA
    • Rasband WS. ImageJ. US National Institute of Health, Bethesda, Maryland, USA 2006.
    • (2006) ImageJ
    • Rasband, W.S.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.