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Volumn 288, Issue 4, 2013, Pages 2223-2237

Phosphatase and tensin homolog (PTEN)-induced Putative Kinase 1 (PINK1)-dependent ubiquitination of endogenous parkin attenuates mitophagy: Study in human primary fibroblasts and induced pluripotent stem cell-derived neurons

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEINS; CELL LINES; CELL MODEL; CELLULAR MODEL; DOSE-DEPENDENT; ENDOGENOUS LEVEL; MITOCHONDRIAL FUNCTION; MITOCHONDRIAL MEMBRANE POTENTIAL; MITOCHONDRIAL PROTEIN; NEURONAL CELL; OUTER MITOCHONDRIAL MEMBRANES; OVER-EXPRESSION; PARKINSON DISEASE; PLURIPOTENT; POLYUBIQUITINATION; UBIQUITIN; UBIQUITIN LIGASES; UBIQUITIN-PROTEASOME SYSTEM; UBIQUITINATION;

EID: 84873843566     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.391680     Document Type: Article
Times cited : (196)

References (35)
  • 1
    • 0020680904 scopus 로고
    • Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis
    • Langston, J. W., Ballard, P., Tetrud, J. W., and Irwin, I. (1983) Chronic Parkinsonism in humans due to a product of meperidine-analog synthesis. Science 219, 979-980
    • (1983) Science , vol.219 , pp. 979-980
    • Langston, J.W.1    Ballard, P.2    Tetrud, J.W.3    Irwin, I.4
  • 5
    • 33745589773 scopus 로고    scopus 로고
    • Drosophila PINK1 is required for mitochondrial function and interacts genetically with Parkin
    • Clark, I. E., Dodson, M. W., Jiang, C., Cao, J. H., Huh, J. R., Seol, J. H., Yoo, S. J., Hay, B. A., and Guo, M. (2006) Drosophila PINK1 is required for mitochondrial function and interacts genetically with Parkin. Nature 441, 1162-1166
    • (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
  • 10
  • 13
    • 79957472437 scopus 로고    scopus 로고
    • Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane
    • Yoshii, S. R., Kishi, C., Ishihara, N., and Mizushima, N. (2011) Parkin mediates proteasome-dependent protein degradation and rupture of the outer mitochondrial membrane. J. Biol. Chem. 286, 19630-19640
    • (2011) J. Biol. Chem. , vol.286 , pp. 19630-19640
    • Yoshii, S.R.1    Kishi, C.2    Ishihara, N.3    Mizushima, N.4
  • 14
    • 79551603345 scopus 로고    scopus 로고
    • Bioenergetics of neurons inhibit the translocation response of Parkin following rapid mitochondrial depolarization
    • Van Laar, V. S., Arnold, B., Cassady, S. J., Chu, C. T., Burton, E. A., and Berman, S. B. (2011) Bioenergetics of neurons inhibit the translocation response of Parkin following rapid mitochondrial depolarization. Hum. Mol. Genet. 20, 927-940
    • (2011) Hum. Mol. Genet. , vol.20 , pp. 927-940
    • Van Laar, V.S.1    Arnold, B.2    Cassady, S.J.3    Chu, C.T.4    Burton, E.A.5    Berman, S.B.6
  • 15
    • 84858701257 scopus 로고    scopus 로고
    • Spatial Parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons
    • Cai, Q., Zakaria, H. M., Simone, A., and Sheng, Z. H. (2012) Spatial Parkin translocation and degradation of damaged mitochondria via mitophagy in live cortical neurons. Curr. Biol. 22, 545-552
    • (2012) Curr. Biol. , vol.22 , pp. 545-552
    • Cai, Q.1    Zakaria, H.M.2    Simone, A.3    Sheng, Z.H.4
  • 16
    • 79955786943 scopus 로고    scopus 로고
    • Mitochondrial Parkin recruitment is impaired in neurons derived from mutant PINK1 induced pluripotent stem cells
    • Seibler, P., Graziotto, J., Jeong, H., Simunovic, F., Klein, C., and Krainc, D. (2011) Mitochondrial Parkin recruitment is impaired in neurons derived from mutant PINK1 induced pluripotent stem cells. J. Neurosci. 31, 5970-5976
    • (2011) J. Neurosci. , vol.31 , pp. 5970-5976
    • Seibler, P.1    Graziotto, J.2    Jeong, H.3    Simunovic, F.4    Klein, C.5    Krainc, D.6
  • 17
    • 0030805969 scopus 로고    scopus 로고
    • Isolation and characterization of tightly coupled mitochondria from neurons and astrocytes in primary culture
    • Almeida, A., and Medina, J. M. (1997) Isolation and characterization of tightly coupled mitochondria from neurons and astrocytes in primary culture. Brain Res. 764, 167-172
    • (1997) Brain Res. , vol.764 , pp. 167-172
    • Almeida, A.1    Medina, J.M.2
  • 22
    • 33644606491 scopus 로고    scopus 로고
    • Tracker dyes to probe mitochondrial autophagy (mitophagy) in rat hepatocytes
    • Rodriguez-Enriquez, S., Kim, I., Currin, R. T., and Lemasters, J. J. (2006) Tracker dyes to probe mitochondrial autophagy (mitophagy) in rat hepatocytes. Autophagy 2, 39-46
    • (2006) Autophagy , vol.2 , pp. 39-46
    • Rodriguez-Enriquez, S.1    Kim, I.2    Currin, R.T.3    Lemasters, J.J.4
  • 23
    • 77955437274 scopus 로고    scopus 로고
    • How could Parkin-mediated ubiquitination of mitofusin promote mitophagy?
    • Ziviani, E., and Whitworth, A. J. (2010) How could Parkin-mediated ubiquitination of mitofusin promote mitophagy? Autophagy 6, 660-662
    • (2010) Autophagy , vol.6 , pp. 660-662
    • Ziviani, E.1    Whitworth, A.J.2
  • 24
    • 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
  • 25
    • 51649124519 scopus 로고    scopus 로고
    • Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation
    • Kundu, M., Lindsten, T., Yang, C. Y., Wu, J., Zhao, F., Zhang, J., Selak, M. A., Ney, P. A., and Thompson, C. B. (2008) Ulk1 plays a critical role in the autophagic clearance of mitochondria and ribosomes during reticulocyte maturation. Blood 112, 1493-1502
    • (2008) Blood , vol.112 , pp. 1493-1502
    • Kundu, M.1    Lindsten, T.2    Yang, C.Y.3    Wu, J.4    Zhao, F.5    Zhang, J.6    Selak, M.A.7    Ney, P.A.8    Thompson, C.B.9
  • 30
    • 27644587453 scopus 로고    scopus 로고
    • Assaying degradation and deubiquitination of a ubiquitinated substrate by purified 26S proteasomes
    • Verma, R., and Deshaies, R. J. (2005) Assaying degradation and deubiquitination of a ubiquitinated substrate by purified 26S proteasomes. Methods Enzymol. 398, 391-399
    • (2005) Methods Enzymol. , vol.398 , pp. 391-399
    • Verma, R.1    Deshaies, R.J.2
  • 31
    • 79952303794 scopus 로고    scopus 로고
    • PARIS (ZNF746) repression of PGC-2011) PARIS (ZNF746) repression1α contributes to neurodegeneration in Parkinson's disease
    • Shin, J. H., Ko, H. S., Kang, H., Lee, Y., Lee, Y. I., Pletinkova, O., Troconso, J. C., Dawson, V. L., and Dawson, T. M. (2011) PARIS (ZNF746) repression of PGC-1α contributes to neurodegeneration in Parkinson's disease. Cell 144, 689-702
    • (2011) Cell , vol.144 , pp. 689-702
    • Shin, J.H.1    Ko, H.S.2    Kang, H.3    Lee, Y.4    Lee, Y.I.5    Pletinkova, O.6    Troconso, J.C.7    Dawson, V.L.8    Dawson, T.M.9
  • 32
    • 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
  • 33
    • 79961239061 scopus 로고    scopus 로고
    • Impaired mitochondrial transport and Parkin-independent degeneration of respiratory chain-deficient dopamine neurons in vivo
    • Sterky, F. H., Lee, S., Wibom, R., Olson, L., and Larsson, N. G. (2011) Impaired mitochondrial transport and Parkin-independent degeneration of respiratory chain-deficient dopamine neurons in vivo. Proc. Natl. Acad. Sci. U.S.A. 108, 12937-12942
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 12937-12942
    • Sterky, F.H.1    Lee, S.2    Wibom, R.3    Olson, L.4    Larsson, N.G.5
  • 34
    • 0024380865 scopus 로고
    • Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein
    • Mizzen, L. A., Chang, C., Garrels, J. I., and Welch, W. J. (1989) Identification, characterization, and purification of two mammalian stress proteins present in mitochondria, grp 75, a member of the hsp 70 family and hsp 58, a homolog of the bacterial groEL protein. J. Biol. Chem. 264, 20664-20675
    • (1989) J. Biol. Chem. , vol.264 , pp. 20664-20675
    • Mizzen, L.A.1    Chang, C.2    Garrels, J.I.3    Welch, W.J.4
  • 35
    • 79953685935 scopus 로고    scopus 로고
    • Alterations in the mitochondrial proteome of neuroblastoma cells in response to complex 1 inhibition
    • Burté, F., De Girolamo, L. A., Hargreaves, A. J., and Billett, E. E. (2011) Alterations in the mitochondrial proteome of neuroblastoma cells in response to complex 1 inhibition. J. Proteome Res. 10, 1974-1986
    • (2011) J. Proteome Res. , vol.10 , pp. 1974-1986
    • Burté, F.1    De Girolamo, L.A.2    Hargreaves, A.J.3    Billett, E.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.