메뉴 건너뛰기




Volumn 24, Issue 16, 2014, Pages 1854-1865

PINK1 triggers autocatalytic activation of parkin to specify cell fate decisions

Author keywords

[No Author keywords available]

Indexed keywords

PARKIN; PROTEIN KINASE; PTEN-INDUCED PUTATIVE KINASE; UBIQUITIN PROTEIN LIGASE;

EID: 84906315018     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2014.07.014     Document Type: Article
Times cited : (85)

References (37)
  • 2
    • 77953424577 scopus 로고    scopus 로고
    • The role of parkin in familial and sporadic Parkinson's disease
    • T.M. Dawson, and V.L. Dawson The role of parkin in familial and sporadic Parkinson's disease Mov. Disord. 25 Suppl 1 2010 S32 S39
    • (2010) Mov. Disord. , vol.25 , Issue.SUPPL. 1
    • Dawson, T.M.1    Dawson, V.L.2
  • 3
    • 22244442489 scopus 로고    scopus 로고
    • The biochemistry of Parkinson's disease
    • M.R. Cookson The biochemistry of Parkinson's disease Annu. Rev. Biochem. 74 2005 29 52
    • (2005) Annu. Rev. Biochem. , vol.74 , pp. 29-52
    • Cookson, M.R.1
  • 5
    • 84901471156 scopus 로고    scopus 로고
    • Parkin and mitochondrial quality control: Toward assembling the puzzle
    • K.F. Winklhofer Parkin and mitochondrial quality control: toward assembling the puzzle Trends Cell Biol. 24 2014 332 341
    • (2014) Trends Cell Biol. , vol.24 , pp. 332-341
    • Winklhofer, K.F.1
  • 6
    • 84868575932 scopus 로고    scopus 로고
    • Mitochondrial quality control mediated by PINK1 and Parkin: Links to parkinsonism
    • D. Narendra, J.E. Walker, and R. Youle Mitochondrial quality control mediated by PINK1 and Parkin: links to parkinsonism Cold Spring Harb. Perspect. Biol. 4 2012 a011338
    • (2012) Cold Spring Harb. Perspect. Biol. , vol.4 , pp. 011338
    • Narendra, D.1    Walker, J.E.2    Youle, R.3
  • 10
    • 84876531457 scopus 로고    scopus 로고
    • PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria
    • Y. Chen, and G.W. Dorn 2nd PINK1-phosphorylated mitofusin 2 is a Parkin receptor for culling damaged mitochondria Science 340 2013 471 475
    • (2013) Science , vol.340 , pp. 471-475
    • Chen, Y.1    Dorn II, G.W.2
  • 13
    • 77951181836 scopus 로고    scopus 로고
    • PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy
    • N. Matsuda, S. Sato, K. Shiba, K. Okatsu, K. Saisho, C.A. Gautier, Y.S. Sou, S. Saiki, S. Kawajiri, and F. Sato et al. PINK1 stabilized by mitochondrial depolarization recruits Parkin to damaged mitochondria and activates latent Parkin for mitophagy J. Cell Biol. 189 2010 211 221
    • (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
  • 15
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • D.M. Wenzel, A. Lissounov, P.S. Brzovic, and R.E. Klevit UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids Nature 474 2011 105 108
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 16
    • 84879885169 scopus 로고    scopus 로고
    • Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism
    • X. Zheng, and T. Hunter Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism Cell Res. 23 2013 886 897
    • (2013) Cell Res. , vol.23 , pp. 886-897
    • Zheng, X.1    Hunter, T.2
  • 17
    • 84873045973 scopus 로고    scopus 로고
    • PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding
    • M. Lazarou, D.P. Narendra, S.M. Jin, E. Tekle, S. Banerjee, and R.J. Youle PINK1 drives Parkin self-association and HECT-like E3 activity upstream of mitochondrial binding J. Cell Biol. 200 2013 163 172
    • (2013) J. Cell Biol. , vol.200 , pp. 163-172
    • Lazarou, M.1    Narendra, D.P.2    Jin, S.M.3    Tekle, E.4    Banerjee, S.5    Youle, R.J.6
  • 18
    • 34548851476 scopus 로고    scopus 로고
    • Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6
    • J.A. Olzmann, L. Li, M.V. Chudaev, J. Chen, F.A. Perez, R.D. Palmiter, and L.S. Chin Parkin-mediated K63-linked polyubiquitination targets misfolded DJ-1 to aggresomes via binding to HDAC6 J. Cell Biol. 178 2007 1025 1038
    • (2007) J. Cell Biol. , vol.178 , pp. 1025-1038
    • Olzmann, J.A.1    Li, L.2    Chudaev, M.V.3    Chen, J.4    Perez, F.A.5    Palmiter, R.D.6    Chin, L.S.7
  • 20
    • 79953231682 scopus 로고    scopus 로고
    • Parkin ubiquitinates Drp1 for proteasome-dependent degradation: Implication of dysregulated mitochondrial dynamics in Parkinson disease
    • H. Wang, P. Song, L. Du, W. Tian, W. Yue, M. Liu, D. Li, B. Wang, Y. Zhu, and C. Cao et al. Parkin ubiquitinates Drp1 for proteasome-dependent degradation: implication of dysregulated mitochondrial dynamics in Parkinson disease J. Biol. Chem. 286 2011 11649 11658
    • (2011) J. Biol. Chem. , vol.286 , pp. 11649-11658
    • Wang, H.1    Song, P.2    Du, L.3    Tian, W.4    Yue, W.5    Liu, M.6    Li, D.7    Wang, B.8    Zhu, Y.9    Cao, C.10
  • 24
    • 84897863239 scopus 로고    scopus 로고
    • Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control
    • G.L. McLelland, V. Soubannier, C.X. Chen, H.M. McBride, and E.A. Fon Parkin and PINK1 function in a vesicular trafficking pathway regulating mitochondrial quality control EMBO J. 33 2014 282 295
    • (2014) EMBO J. , vol.33 , pp. 282-295
    • McLelland, G.L.1    Soubannier, V.2    Chen, C.X.3    McBride, H.M.4    Fon, E.A.5
  • 26
    • 58149314211 scopus 로고    scopus 로고
    • Parkin is recruited selectively to impaired mitochondria and promotes their autophagy
    • D. Narendra, A. Tanaka, D.-F. Suen, and R.J. Youle Parkin is recruited selectively to impaired mitochondria and promotes their autophagy J. Cell Biol. 183 2008 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
  • 27
    • 49649097747 scopus 로고    scopus 로고
    • Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress
    • C.A. Gautier, T. Kitada, and J. Shen Loss of PINK1 causes mitochondrial functional defects and increased sensitivity to oxidative stress Proc. Natl. Acad. Sci. USA 105 2008 11364 11369
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 11364-11369
    • Gautier, C.A.1    Kitada, T.2    Shen, J.3
  • 29
    • 84880303306 scopus 로고    scopus 로고
    • PINK1 protects against cell death induced by mitochondrial depolarization, by phosphorylating Bcl-xL and impairing its pro-apoptotic cleavage
    • G. Arena, V. Gelmetti, L. Torosantucci, D. Vignone, G. Lamorte, P. De Rosa, E. Cilia, E.A. Jonas, and E.M. Valente PINK1 protects against cell death induced by mitochondrial depolarization, by phosphorylating Bcl-xL and impairing its pro-apoptotic cleavage Cell Death Differ. 20 2013 920 930
    • (2013) Cell Death Differ. , vol.20 , pp. 920-930
    • Arena, G.1    Gelmetti, V.2    Torosantucci, L.3    Vignone, D.4    Lamorte, G.5    De Rosa, P.6    Cilia, E.7    Jonas, E.A.8    Valente, E.M.9
  • 30
    • 84882754147 scopus 로고    scopus 로고
    • A neo-substrate that amplifies catalytic activity of parkinson's-disease- related kinase PINK1
    • N.T. Hertz, A. Berthet, M.L. Sos, K.S. Thorn, A.L. Burlingame, K. Nakamura, and K.M. Shokat A neo-substrate that amplifies catalytic activity of parkinson's-disease-related kinase PINK1 Cell 154 2013 737 747
    • (2013) Cell , vol.154 , pp. 737-747
    • Hertz, N.T.1    Berthet, A.2    Sos, M.L.3    Thorn, K.S.4    Burlingame, A.L.5    Nakamura, K.6    Shokat, K.M.7
  • 33
    • 27644466759 scopus 로고    scopus 로고
    • Autophagy and signaling: Their role in cell survival and cell death
    • P. Codogno, and A.J. Meijer Autophagy and signaling: their role in cell survival and cell death Cell Death Differ. 12 Suppl 2 2005 1509 1518
    • (2005) Cell Death Differ. , vol.12 , Issue.SUPPL. 2 , pp. 1509-1518
    • Codogno, P.1    Meijer, A.J.2
  • 34
    • 21244472965 scopus 로고    scopus 로고
    • Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis
    • Q. Zhong, W. Gao, F. Du, and X. Wang Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis Cell 121 2005 1085 1095
    • (2005) Cell , vol.121 , pp. 1085-1095
    • Zhong, Q.1    Gao, W.2    Du, F.3    Wang, X.4
  • 37
    • 24044471278 scopus 로고    scopus 로고
    • Ubiquitination of p27Kip1 requires physical interaction with cyclin e and probable phosphate recognition by SKP2
    • D. Ungermannova, Y. Gao, and X. Liu Ubiquitination of p27Kip1 requires physical interaction with cyclin E and probable phosphate recognition by SKP2 J. Biol. Chem. 280 2005 30301 30309
    • (2005) J. Biol. Chem. , vol.280 , pp. 30301-30309
    • Ungermannova, D.1    Gao, Y.2    Liu, X.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.