메뉴 건너뛰기




Volumn 200, Issue 2, 2013, Pages 163-172

PINK1 drives parkin self-association and HECT-like E3 activity upstream of mitochondrial binding

Author keywords

[No Author keywords available]

Indexed keywords

MITOCHONDRIAL ENZYME; MITOFUSIN 1; MUTANT PROTEIN; PARKIN; PINK1 PROTEIN; THIOESTER; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84873045973     PISSN: 00219525     EISSN: 15408140     Source Type: Journal    
DOI: 10.1083/jcb.201210111     Document Type: Article
Times cited : (202)

References (40)
  • 1
    • 17644365438 scopus 로고    scopus 로고
    • Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability
    • Beilina, A., M. Van Der Brug, R. Ahmad, S. Kesavapany, D.W. Miller, G.A. Petsko, and M.R. Cookson. 2005. Mutations in PTEN-induced putative kinase 1 associated with recessive parkinsonism have differential effects on protein stability. Proc. Natl. Acad. Sci. USA. 102:5703-5708. http:// dx.doi.org/10.1073/pnas.0500617102
    • (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    Cookson, M.R.7
  • 3
    • 79960649509 scopus 로고    scopus 로고
    • Autoregulation of Parkin activity through its ubiquitinlike domain
    • Chaugule, V.K., L. Burchell, K.R. Barber, A. Sidhu, S.J. Leslie, G.S. Shaw, and H. Walden. 2011. Autoregulation of Parkin activity through its ubiquitinlike domain. EMBO J. 30:2853-2867. http://dx.doi.org/10.1038/emboj .2011.204
    • (2011) EMBO J. , vol.30 , pp. 2853-2867
    • Chaugule, V.K.1    Burchell, L.2    Barber, K.R.3    Sidhu, A.4    Leslie, S.J.5    Shaw, G.S.6    Walden, H.7
  • 4
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin
    • Clark, I.E., M.W. Dodson, C. Jiang, J.H. Cao, J.R. Huh, J.H. Seol, S.J. Yoo, B.A. Hay, and M. Guo. 2006. Drosophila pink1 is required for mitochondrial function and interacts genetically with parkin. Nature. 441:1162-1166. http://dx.doi.org/10.1038/nature04779
    • (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    Yoo, S.J.7    Hay, B.A.8    Guo, M.9
  • 7
    • 0344441899 scopus 로고    scopus 로고
    • Alterations in the common fragile site gene Parkin in ovarian and other cancers
    • Denison, S.R., F. Wang, N.A. Becker, B. Schüle, N. Kock, L.A. Phillips, C. Klein, and D.I. Smith. 2003. Alterations in the common fragile site gene Parkin in ovarian and other cancers. Oncogene. 22:8370-8378. http:// dx.doi.org/10.1038/sj.onc.1207072
    • (2003) Oncogene , vol.22 , pp. 8370-8378
    • Denison, S.R.1    Wang, F.2    Becker, N.A.3    Schüle, B.4    Kock, N.5    Phillips, L.A.6    Klein, C.7    Smith, D.I.8
  • 8
    • 78649463381 scopus 로고    scopus 로고
    • Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy
    • Gegg, M.E., J.M. Cooper, K.Y. Chau, M. Rojo, A.H. Schapira, and J.W. Taanman. 2010. Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/parkin-dependent manner upon induction of mitophagy. Hum. Mol. Genet. 19:4861-4870. http://dx.doi.org/10.1093/hmg/ddq419
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 4861-4870
    • Gegg, M.E.1    Cooper, J.M.2    Chau, K.Y.3    Rojo, M.4    Schapira, A.H.5    Taanman, J.W.6
  • 11
    • 33745280651 scopus 로고    scopus 로고
    • Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacity
    • Hampe, C., H. Ardila-Osorio, M. Fournier, A. Brice, and O. Corti. 2006. Biochemical analysis of Parkinson's disease-causing variants of Parkin, an E3 ubiquitin-protein ligase with monoubiquitylation capacity. Hum. Mol. Genet. 15:2059-2075. http://dx.doi.org/10.1093/hmg/ddl131
    • (2006) Hum. Mol. Genet. , vol.15 , pp. 2059-2075
    • Hampe, C.1    Ardila-Osorio, H.2    Fournier, M.3    Brice, A.4    Corti, O.5
  • 12
    • 34347237194 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy: novel variations of an established technique
    • Haustein, E., and P. Schwille. 2007. Fluorescence correlation spectroscopy: novel variations of an established technique. Annu. Rev. Biophys. Biomol. Struct. 36:151-169. http://dx.doi.org/10.1146/annurev.biophys.36.040306 .132612
    • (2007) Annu. Rev. Biophys. Biomol. Struct. , vol.36 , pp. 151-169
    • Haustein, E.1    Schwille, P.2
  • 13
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
    • Jin, S.M., M. Lazarou, C. Wang, L.A. Kane, D.P. Narendra, and R.J. Youle. 2010. Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J. Cell Biol. 191:933-942. http:// dx.doi.org/10.1083/jcb.201008084
    • (2010) J. Cell Biol. , vol.191 , pp. 933-942
    • Jin, S.M.1    Lazarou, M.2    Wang, C.3    Kane, L.A.4    Narendra, D.P.5    Youle, R.J.6
  • 14
    • 0037180485 scopus 로고    scopus 로고
    • Control of biochemical reactions through supramolecular RING domain self-assembly
    • Kentsis, A., R.E. Gordon, and K.L. Borden. 2002. Control of biochemical reactions through supramolecular RING domain self-assembly. Proc. Natl. Acad. Sci. USA. 99:15404-15409. http://dx.doi.org/10.1073/pnas.202608799
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 15404-15409
    • Kentsis, A.1    Gordon, R.E.2    Borden, K.L.3
  • 15
    • 35748946937 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy in living cells
    • Kim, S.A., K.G. Heinze, and P. Schwille. 2007. Fluorescence correlation spectroscopy in living cells. Nat. Methods. 4:963-973. http://dx.doi.org/10 .1038/nmeth1104
    • (2007) Nat. Methods , vol.4 , pp. 963-973
    • Kim, S.A.1    Heinze, K.G.2    Schwille, P.3
  • 17
    • 84864267876 scopus 로고    scopus 로고
    • PINK1 is activated by mitochondrial membrane potential depolarization and stimulates Parkin E3 ligase activity by phosphorylating Serine 65
    • Kondapalli, C., A. Kazlauskaite, N. Zhang, H.I. Woodroof, D.G. Campbell, R. Gourlay, L. Burchell, H. Walden, T.J. Macartney, M. Deak, 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. http://dx.doi.org/10.1098/rsob.120080
    • (2012) Open Biol. , vol.2 , pp. 120080
    • Kondapalli, C.1    Kazlauskaite, A.2    Zhang, N.3    Woodroof, H.I.4    Campbell, D.G.5    Gourlay, R.6    Burchell, L.7    Walden, H.8    Macartney, T.J.9    Deak, M.10
  • 18
    • 84870302181 scopus 로고    scopus 로고
    • MitoNEET-driven alterations in adipocyte mitochondrial activity reveal a crucial adaptive process that preserves insulin sensitivity in obesity
    • Kusminski, C.M., W.L. Holland, K. Sun, J. Park, S.B. Spurgin, Y. Lin, G.R. Askew, J.A. Simcox, D.A. McClain, C. Li, and P.E. Scherer. 2012. MitoNEET-driven alterations in adipocyte mitochondrial activity reveal a crucial adaptive process that preserves insulin sensitivity in obesity. Nat. Med. 18:1539-1549. http://dx.doi.org/10.1038/nm.2899
    • (2012) Nat. Med. , vol.18 , pp. 1539-1549
    • Kusminski, C.M.1    Holland, W.L.2    Sun, K.3    Park, J.4    Spurgin, S.B.5    Lin, Y.6    Askew, G.R.7    Simcox, J.A.8    Mcclain, D.A.9    Li, C.10    Scherer, P.E.11
  • 19
    • 84857032953 scopus 로고    scopus 로고
    • Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin
    • Lazarou, M., S.M. Jin, L.A. Kane, and R.J. Youle. 2012. Role of PINK1 binding to the TOM complex and alternate intracellular membranes in recruitment and activation of the E3 ligase Parkin. Dev. Cell. 22:320-333. http://dx.doi.org/10.1016/j.devcel.2011.12.014
    • (2012) Dev. Cell , vol.22 , pp. 320-333
    • Lazarou, M.1    Jin, S.M.2    Kane, L.A.3    Youle, R.J.4
  • 20
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • Matsuda, N., S. Sato, K. Shiba, K. Okatsu, K. Saisho, C.A. Gautier, Y.-S. Sou, S. Saiki, S. Kawajiri, F. Sato, et al. 2010. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy. J. Cell Biol. 189:211-221. http://dx.doi .org/10.1083/jcb.200910140
    • (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    Sou, Y.-S.7    Saiki, S.8    Kawajiri, S.9    Sato, F.10
  • 21
    • 79955667485 scopus 로고    scopus 로고
    • The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking
    • Meissner, C., H. Lorenz, A. Weihofen, D.J. Selkoe, and M.K. Lemberg. 2011. The mitochondrial intramembrane protease PARL cleaves human Pink1 to regulate Pink1 trafficking. J. Neurochem. 117:856-867. http://dx.doi.org/ 10.1111/j.1471-4159.2011.07253.x
    • (2011) J. Neurochem , vol.117 , pp. 856-867
    • Meissner, C.1    Lorenz, H.2    Weihofen, A.3    Selkoe, D.J.4    Lemberg, M.K.5
  • 22
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra, D., A. Tanaka, D.F. Suen, and R.J. Youle. 2008. Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 183:795-803. http://dx.doi.org/10.1083/jcb.200809125
    • (2008) J. Cell Biol. , vol.183 , pp. 795-803
    • Narendra, D.1    Tanaka, A.2    Suen, D.F.3    Youle, R.J.4
  • 24
    • 84868575932 scopus 로고    scopus 로고
    • Mitochondrial quality control mediated by PINK1 and Parkin: links to Parkinsonism
    • Narendra, D.P., J.E. Walker, and R.J. Youle. 2012. Mitochondrial quality control mediated by PINK1 and Parkin: links to Parkinsonism. Cold Spring Harb. Perspect. Biol. 4:a011338. http://dx.doi.org/10.1101/cshperspect. a011338
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4
    • Narendra, D.P.1    Walker, J.E.2    Youle, R.J.3
  • 26
    • 77954104112 scopus 로고    scopus 로고
    • Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update
    • Nuytemans, K., J. Theuns, M. Cruts, and C. Van Broeckhoven. 2010. Genetic etiology of Parkinson disease associated with mutations in the SNCA, PARK2, PINK1, PARK7, and LRRK2 genes: a mutation update. Hum. Mutat. 31:763-780. http://dx.doi.org/10.1002/humu.21277
    • (2010) Hum. Mutat. , vol.31 , pp. 763-780
    • Nuytemans, K.1    Theuns, J.2    Cruts, M.3    Van Broeckhoven, C.4
  • 27
    • 33745602748 scopus 로고    scopus 로고
    • Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin
    • Park, J., S.B. Lee, S. Lee, Y. Kim, S. Song, S. Kim, E. Bae, J. Kim, M. Shong, J.M. Kim, and J. Chung. 2006. Mitochondrial dysfunction in Drosophila PINK1 mutants is complemented by parkin. Nature. 441:1157-1161. http://dx.doi.org/10.1038/nature04788
    • (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    Bae, E.7    Kim, J.8    Shong, M.9    Kim, J.M.10    Chung, J.11
  • 28
    • 77955844260 scopus 로고    scopus 로고
    • The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/ parkin pathway
    • Poole, A.C., R.E. Thomas, S. Yu, E.S. Vincow, and L. Pallanck. 2010. The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/ parkin pathway. PLoS ONE. 5:e10054. http://dx.doi.org/10.1371/journal .pone.0010054
    • (2010) PLoS ONE , vol.5
    • Poole, A.C.1    Thomas, R.E.2    Yu, S.3    Vincow, E.S.4    Pallanck, L.5
  • 30
    • 78650729600 scopus 로고    scopus 로고
    • Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin
    • Tanaka, A., M.M. Cleland, S. Xu, D.P. Narendra, D.F. Suen, M. Karbowski, and R.J. Youle. 2010. Proteasome and p97 mediate mitophagy and degradation of mitofusins induced by Parkin. J. Cell Biol. 191:1367-1380. http:// dx.doi.org/10.1083/jcb.201007013
    • (2010) J. Cell Biol. , vol.191 , pp. 1367-1380
    • Tanaka, A.1    Cleland, M.M.2    Xu, S.3    Narendra, D.P.4    Suen, D.F.5    Karbowski, M.6    Youle, R.J.7
  • 32
    • 30144439025 scopus 로고    scopus 로고
    • The Prp19 U-box crystal structure suggests a common dimeric architecture for a class of oligomeric E3 ubiquitin ligases
    • Vander Kooi, C.W., M.D. Ohi, J.A. Rosenberg, M.L. Oldham, M.E. Newcomer, K.L. Gould, and W.J. Chazin. 2006. The Prp19 U-box crystal structure suggests a common dimeric architecture for a class of oligomeric E3 ubiquitin ligases. Biochemistry. 45:121-130. http://dx.doi.org/10.1021/ bi051787e
    • (2006) Biochemistry , vol.45 , pp. 121-130
    • Vander Kooi, C.W.1    Ohi, M.D.2    Rosenberg, J.A.3    Oldham, M.L.4    Newcomer, M.E.5    Gould, K.L.6    Chazin, W.J.7
  • 34
    • 2442715340 scopus 로고    scopus 로고
    • Fluorescence correlation spectroscopy investigation of a GFP mutant-enhanced cyan fluorescent protein and its tubulin fusion in living cells with two-photon excitation
    • Wang, Z., J.V. Shah, Z. Chen, C.H. Sun, and M.W. Berns. 2004. Fluorescence correlation spectroscopy investigation of a GFP mutant-enhanced cyan fluorescent protein and its tubulin fusion in living cells with two-photon excitation. J. Biomed. Opt. 9:395-403. http://dx.doi.org/10.1117/1.1646416
    • (2004) J. Biomed. Opt. , vol.9 , pp. 395-403
    • Wang, Z.1    Shah, J.V.2    Chen, Z.3    Sun, C.H.4    Berns, M.W.5
  • 35
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • Wenzel, D.M., A. Lissounov, P.S. Brzovic, and R.E. Klevit. 2011. UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature. 474:105-108. http://dx.doi.org/10.1038/nature09966
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 36
    • 58149397651 scopus 로고    scopus 로고
    • Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin
    • discussion :173
    • Whitworth, A.J., J.R. Lee, V.M. Ho, R. Flick, R. Chowdhury, and G.A. McQuibban. 2008. Rhomboid-7 and HtrA2/Omi act in a common pathway with the Parkinson's disease factors Pink1 and Parkin. Dis Model Mech. 1:168-174, discussion :173. http://dx.doi.org/10.1242/dmm.000109
    • (2008) Dis Model Mech. , vol.1 , pp. 168-174
    • Whitworth, A.J.1    Lee, J.R.2    Ho, V.M.3    Flick, R.4    Chowdhury, R.5    Mcquibban, G.A.6
  • 37
    • 33746080412 scopus 로고    scopus 로고
    • Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin
    • Yang, Y., S. Gehrke, Y. Imai, Z. Huang, Y. Ouyang, J.W. Wang, L. Yang, M.F. Beal, H. Vogel, and B. Lu. 2006. Mitochondrial pathology and muscle and dopaminergic neuron degeneration caused by inactivation of Drosophila Pink1 is rescued by Parkin. Proc. Natl. Acad. Sci. USA. 103:10793-10798. http://dx.doi.org/10.1073/pnas.0602493103
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 10793-10798
    • Yang, Y.1    Gehrke, S.2    Imai, Y.3    Huang, Z.4    Ouyang, Y.5    Wang, J.W.6    Yang, L.7    Beal, M.F.8    Vogel, H.9    Lu, B.10
  • 39
    • 79957472437 scopus 로고    scopus 로고
    • Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane
    • Yoshii, S.R., C. Kishi, N. Ishihara, and N. Mizushima. 2011. Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane. J. Biol. Chem. 286:19630-19640. http://dx.doi.org/ 10.1074/jbc.M110.209338
    • (2011) J. Biol. Chem. , vol.286 , pp. 19630-19640
    • Yoshii, S.R.1    Kishi, C.2    Ishihara, N.3    Mizushima, N.4
  • 40
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani, E., R.N. Tao, and A.J. Whitworth. 2010. Drosophila parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. USA. 107:5018-5023. http://dx.doi.org/10.1073/pnas .0913485107
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.