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Volumn 287, Issue 48, 2012, Pages 40652-40660

Voltage-dependent anion channels (VDACs) recruit parkin to defective mitochondria to promote mitochondrial autophagy

Author keywords

[No Author keywords available]

Indexed keywords

AUTOPHAGY; CYTOSOLS; DOCKING SITES; OUTER MITOCHONDRIAL MEMBRANES; PARKINSON DISEASE; PORE-FORMING PROTEINS; UBIQUITIN LIGASES; UNCOUPLERS; VOLTAGE-DEPENDENT ANION CHANNELS;

EID: 84870013071     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.419721     Document Type: Article
Times cited : (187)

References (33)
  • 1
    • 79954577302 scopus 로고    scopus 로고
    • Targeting mitochondrial dysfunction: Role for PINK1 and Parkin in mitochondrial quality control
    • Narendra, D. P., and Youle, R. J. (2011) Targeting mitochondrial dysfunction: role for PINK1 and Parkin in mitochondrial quality control. Antioxid. Redox Signal. 14, 1929-1938
    • (2011) Antioxid. Redox Signal. , vol.14 , pp. 1929-1938
    • Narendra, D.P.1    Youle, R.J.2
  • 2
    • 79952324644 scopus 로고    scopus 로고
    • Regulation of PINK1-Parkin-mediated mitophagy
    • Springer, W., and Kahle, P. J. (2011) Regulation of PINK1-Parkin-mediated mitophagy. Autophagy 7, 266-278
    • (2011) Autophagy , vol.7 , pp. 266-278
    • Springer, W.1    Kahle, P.J.2
  • 3
    • 33750347347 scopus 로고    scopus 로고
    • Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases
    • DOI 10.1038/nature05292, PII NATURE05292
    • Lin, M. T., and Beal, M. F. (2006) Mitochondrial dysfunction and oxidative stress in neurodegenerative diseases. Nature 443, 787-795 (Pubitemid 44622683)
    • (2006) Nature , vol.443 , Issue.7113 , pp. 787-795
    • Lin, M.T.1    Beal, M.F.2
  • 4
    • 79959305691 scopus 로고    scopus 로고
    • Mitochondria: The next (neurode) generation
    • Schon, E. A., and Przedborski, S. (2011) Mitochondria: the next (neurode) generation. Neuron 70, 1033-1053
    • (2011) Neuron , vol.70 , pp. 1033-1053
    • Schon, E.A.1    Przedborski, S.2
  • 5
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • Narendra, D., Tanaka, A., Suen, D. F., and Youle, R. J. (2008) Parkin is recruited selectively to impaired mitochondria and promotes their autophagy. J. Cell Biol. 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
  • 8
    • 77950384477 scopus 로고    scopus 로고
    • Drosophila Parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin
    • Ziviani, E., Tao, R. N., and Whitworth, A. J. (2010) Drosophila Parkin requires PINK1 for mitochondrial translocation and ubiquitinates mitofusin. Proc. Natl. Acad. Sci. U.S.A. 107, 5018-5023
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 5018-5023
    • Ziviani, E.1    Tao, R.N.2    Whitworth, A.J.3
  • 9
    • 77955844260 scopus 로고    scopus 로고
    • The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/Parkin pathway
    • Poole, A. C., Thomas, R. E., Yu, S., Vincow, E. S., and Pallanck, L. (2010) The mitochondrial fusion-promoting factor mitofusin is a substrate of the PINK1/Parkin pathway. PLoS One 5, e10054
    • (2010) PLoS One , vol.5
    • Poole, A.C.1    Thomas, R.E.2    Yu, S.3    Vincow, E.S.4    Pallanck, L.5
  • 10
    • 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., Cooper, J. M., Chau, K. Y., Rojo, M., Schapira, A. H., and Taanman, J. W. (2010) Mitofusin 1 and mitofusin 2 are ubiquitinated in a PINK1/Parkin-dependent manner upon induction of mitophagy. Hum. Mol. Genet. 19, 4861-4870
    • (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
  • 13
    • 79960493052 scopus 로고    scopus 로고
    • Parkin promotes the ubiquitination and degradation of the mitochondrial fusion factor mitofusin 1
    • Glauser, L., Sonnay, S., Stafa, K., and Moore, D. J. (2011) Parkin promotes the ubiquitination and degradation of the mitochondrial fusion factor mitofusin 1. J. Neurochem. 118, 636-645
    • (2011) J. Neurochem. , vol.118 , pp. 636-645
    • Glauser, L.1    Sonnay, S.2    Stafa, K.3    Moore, D.J.4
  • 14
    • 79952451427 scopus 로고    scopus 로고
    • Mitophagy: The latest problem for Parkinson's disease
    • Vives-Bauza, C., and Przedborski, S. (2011) Mitophagy: the latest problem for Parkinson's disease. Trends Mol. Med. 17, 158-165
    • (2011) Trends Mol. Med. , vol.17 , pp. 158-165
    • Vives-Bauza, C.1    Przedborski, S.2
  • 18
    • 78649300971 scopus 로고    scopus 로고
    • P62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both
    • Narendra, D., Kane, L. A., Hauser, D. N., Fearnley, I. M., and Youle, R. J. (2010) p62/SQSTM1 is required for Parkin-induced mitochondrial clustering but not mitophagy; VDAC1 is dispensable for both. Autophagy 6, 1090-1106
    • (2010) Autophagy , vol.6 , pp. 1090-1106
    • Narendra, D.1    Kane, L.A.2    Hauser, D.N.3    Fearnley, I.M.4    Youle, R.J.5
  • 19
    • 84857850213 scopus 로고    scopus 로고
    • Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy
    • Itakura, E., Kishi-Itakura, C., Koyama-Honda, I., and Mizushima, N. (2012) Structures containing Atg9A and the ULK1 complex independently target depolarized mitochondria at initial stages of Parkin-mediated mitophagy. J. Cell Sci. 125, 1488-1499
    • (2012) J. Cell Sci. , vol.125 , pp. 1488-1499
    • Itakura, E.1    Kishi-Itakura, C.2    Koyama-Honda, I.3    Mizushima, N.4
  • 21
    • 78649685455 scopus 로고    scopus 로고
    • Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL
    • Jin, S. M., Lazarou, M., Wang, C., Kane, L. A., Narendra, D. P., and Youle, R. J. (2010) Mitochondrial membrane potential regulates PINK1 import and proteolytic destabilization by PARL. J. Cell Biol. 191, 933-942
    • (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
  • 24
    • 0034046944 scopus 로고    scopus 로고
    • Plat-E: An efficient and stable system for transient packaging of retroviruses
    • Morita, S., Kojima, T., and Kitamura, T. (2000) Plat-E: an efficient and stable system for transient packaging of retroviruses. Gene Ther. 7, 1063-1066 (Pubitemid 30398356)
    • (2000) Gene Therapy , vol.7 , Issue.12 , pp. 1063-1066
    • Morita, S.1    Kojima, T.2    Kitamura, T.3
  • 26
    • 33750699996 scopus 로고    scopus 로고
    • Analyzing chromatin remodeling complexes using shotgun proteomics and normalized spectral abundance factors
    • DOI 10.1016/j.ymeth.2006.07.028, PII S1046202306002076
    • Florens, L., Carozza, M. J., Swanson, S. K., Fournier, M., Coleman, M. K., Workman, J. L., and Washburn, M. P. (2006) Analyzing chromatin remodeling complexes using shotgun proteomics and normalized spectral abundance factors. Methods 40, 303-311 (Pubitemid 44709624)
    • (2006) Methods , vol.40 , Issue.4 , pp. 303-311
    • Florens, L.1    Carozza, M.J.2    Swanson, S.K.3    Fournier, M.4    Coleman, M.K.5    Workman, J.L.6    Washburn, M.P.7
  • 27
    • 84856510610 scopus 로고    scopus 로고
    • VDAC, a multi-functional mitochondrial protein as a pharmacological target
    • Shoshan-Barmatz, V., and Ben-Hail, D. (2012) VDAC, a multi-functional mitochondrial protein as a pharmacological target. Mitochondrion 12, 23-34
    • (2012) Mitochondrion , vol.12 , pp. 23-34
    • Shoshan-Barmatz, V.1    Ben-Hail, D.2
  • 28
    • 34247895697 scopus 로고    scopus 로고
    • Voltage-dependent anion channels are dispensable for mitochondrial- dependent cell death
    • DOI 10.1038/ncb1575, PII NCB1575
    • Baines, C. P., Kaiser, R. A., Sheiko, T., Craigen, W. J., and Molkentin, J. D. (2007) Voltage-dependent anion channels are dispensable for mitochondrial- dependent cell death. Nat. Cell Biol. 9, 550-555 (Pubitemid 46696536)
    • (2007) Nature Cell Biology , vol.9 , Issue.5 , pp. 550-555
    • Baines, C.P.1    Kaiser, R.A.2    Sheiko, T.3    Craigen, W.J.4    Molkentin, J.D.5
  • 30
    • 77949478474 scopus 로고    scopus 로고
    • Phosphorylation of Parkin by Parkinson disease-linked kinase PINK1 activates Parkin E3 ligase function and NF-κB signaling
    • Sha, D., Chin, L. S., and Li, L. (2010) Phosphorylation of Parkin by Parkinson disease-linked kinase PINK1 activates Parkin E3 ligase function and NF-κB signaling. Hum. Mol. Genet. 19, 352-363
    • (2010) Hum. Mol. Genet. , vol.19 , pp. 352-363
    • Sha, D.1    Chin, L.S.2    Li, L.3
  • 31
    • 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., Jin, S. M., Kane, L. A., and Youle, R. J. (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
    • (2012) Dev. Cell , vol.22 , pp. 320-333
    • Lazarou, M.1    Jin, S.M.2    Kane, L.A.3    Youle, R.J.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.