메뉴 건너뛰기




Volumn 34, Issue 20, 2015, Pages 2506-2521

Disruption of the autoinhibited state primes the E3 ligase parkin for activation and catalysis

Author keywords

enzyme mechanism; Parkinson's disease; phosphorylation; ubiquitin ligase; ubiquitination

Indexed keywords

PARKIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE;

EID: 84944441665     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201592337     Document Type: Article
Times cited : (152)

References (46)
  • 1
    • 33847688139 scopus 로고    scopus 로고
    • Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease
    • Beasley SA, Hristova VA, Shaw GS, (2007) Structure of the Parkin in-between-ring domain provides insights for E3-ligase dysfunction in autosomal recessive Parkinson's disease. Proc Natl Acad Sci USA 104: 3095-3100
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 3095-3100
    • Beasley, S.A.1    Hristova, V.A.2    Shaw, G.S.3
  • 4
    • 84859371301 scopus 로고    scopus 로고
    • Small, N-terminal tags activate Parkin E3 ubiquitin ligase activity by disrupting its autoinhibited conformation
    • Burchell L, Chaugule VK, Walden H, (2012) Small, N-terminal tags activate Parkin E3 ubiquitin ligase activity by disrupting its autoinhibited conformation. PLoS One 7: e34748
    • (2012) PLoS One , vol.7 , pp. e34748
    • Burchell, L.1    Chaugule, V.K.2    Walden, H.3
  • 5
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4.
    • CCP4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 9
    • 0037442962 scopus 로고    scopus 로고
    • HADDOCK: A protein-protein docking approach based on biochemical or biophysical information
    • Dominguez C, Boelens R, Bonvin AM, (2003) HADDOCK: a protein-protein docking approach based on biochemical or biophysical information. J Am Chem Soc 125: 1731-1737
    • (2003) J Am Chem Soc , vol.125 , pp. 1731-1737
    • Dominguez, C.1    Boelens, R.2    Bonvin, A.M.3
  • 10
    • 84878840303 scopus 로고    scopus 로고
    • Structure of HHARI, a RING-IBR-RING ubiquitin ligase: Autoinhibition of an Ariadne-family E3 and insights into ligation mechanism
    • Duda DM, Olszewski JL, Schuermann JP, Kurinov I, Miller DJ, Nourse A, Alpi AF, Schulman BA, (2013) Structure of HHARI, a RING-IBR-RING ubiquitin ligase: autoinhibition of an Ariadne-family E3 and insights into ligation mechanism. Structure 21: 1030-1041
    • (2013) Structure , vol.21 , pp. 1030-1041
    • Duda, D.M.1    Olszewski, J.L.2    Schuermann, J.P.3    Kurinov, I.4    Miller, D.J.5    Nourse, A.6    Alpi, A.F.7    Schulman, B.A.8
  • 11
  • 15
    • 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, Ardila-Osorio H, Fournier M, Brice A, Corti O, (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
    • (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
  • 16
    • 67649383293 scopus 로고    scopus 로고
    • 2+-binding domain in the autosomal recessive juvenile Parkinson-related E3 ligase parkin
    • 2+-binding domain in the autosomal recessive juvenile Parkinson-related E3 ligase parkin. J Biol Chem 284: 14978-14986
    • (2009) J Biol Chem , vol.284 , pp. 14978-14986
    • Hristova, V.A.1    Beasley, S.A.2    Rylett, R.J.3    Shaw, G.S.4
  • 17
    • 34249765651 scopus 로고
    • NMR View: A computer program for the visualization and analysis of NMR data
    • Johnson BA, Blevins RA, (1994) NMR View: a computer program for the visualization and analysis of NMR data. J Biomol NMR 4: 603-614
    • (1994) J Biomol NMR , vol.4 , pp. 603-614
    • Johnson, B.A.1    Blevins, R.A.2
  • 27
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • Pervushin K, Riek R, Wider G, Wuthrich K, (1997) Attenuated T2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution. Proc Natl Acad Sci USA 94: 12366-12371
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 29
    • 84865781586 scopus 로고    scopus 로고
    • Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
    • Plechanovova A, Jaffray EG, Tatham MH, Naismith JH, Hay RT, (2012) Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489: 115-120
    • (2012) Nature , vol.489 , pp. 115-120
    • Plechanovova, A.1    Jaffray, E.G.2    Tatham, M.H.3    Naismith, J.H.4    Hay, R.T.5
  • 31
    • 37049004798 scopus 로고    scopus 로고
    • A disease state mutation unfolds the parkin ubiquitin-like domain
    • Safadi SS, Shaw GS, (2007) A disease state mutation unfolds the parkin ubiquitin-like domain. Biochemistry 46: 14162-14169
    • (2007) Biochemistry , vol.46 , pp. 14162-14169
    • Safadi, S.S.1    Shaw, G.S.2
  • 32
    • 79953182301 scopus 로고    scopus 로고
    • Impact of autosomal recessive juvenile Parkinson's disease mutations on the structure and interactions of the parkin ubiquitin-like domain
    • Safadi SS, Barber KR, Shaw GS, (2011) Impact of autosomal recessive juvenile Parkinson's disease mutations on the structure and interactions of the parkin ubiquitin-like domain. Biochemistry 50: 2603-2610
    • (2011) Biochemistry , vol.50 , pp. 2603-2610
    • Safadi, S.S.1    Barber, K.R.2    Shaw, G.S.3
  • 33
    • 84871891737 scopus 로고    scopus 로고
    • PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy
    • Shiba-Fukushima K, Imai Y, Yoshida S, Ishihama Y, Kanao T, Sato S, Hattori N, (2012) PINK1-mediated phosphorylation of the Parkin ubiquitin-like domain primes mitochondrial translocation of Parkin and regulates mitophagy. Sci Rep 2: 1002
    • (2012) Sci Rep , vol.2 , pp. 1002
    • Shiba-Fukushima, K.1    Imai, Y.2    Yoshida, S.3    Ishihama, Y.4    Kanao, T.5    Sato, S.6    Hattori, N.7
  • 34
    • 84903485895 scopus 로고    scopus 로고
    • PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila
    • Shiba-Fukushima K, Inoshita T, Hattori N, Imai Y, (2014) PINK1-mediated phosphorylation of Parkin boosts Parkin activity in Drosophila. PLoS Genet 10: e1004391
    • (2014) PLoS Genet , vol.10 , pp. e1004391
    • Shiba-Fukushima, K.1    Inoshita, T.2    Hattori, N.3    Imai, Y.4
  • 35
    • 84867096523 scopus 로고    scopus 로고
    • The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension
    • Smit JJ, Monteferrario D, Noordermeer SM, van Dijk WJ, van der Reijden BA, Sixma TK, (2012) The E3 ligase HOIP specifies linear ubiquitin chain assembly through its RING-IBR-RING domain and the unique LDD extension. EMBO J 31: 3833-3844
    • (2012) EMBO J , vol.31 , pp. 3833-3844
    • Smit, J.J.1    Monteferrario, D.2    Noordermeer, S.M.3    Van Dijk, W.J.4    Van Der Reijden, B.A.5    Sixma, T.K.6
  • 37
    • 84896870884 scopus 로고    scopus 로고
    • RBR E3 ubiquitin ligases: New structures, new insights, new questions
    • Spratt DE, Walden H, Shaw GS, (2014) RBR E3 ubiquitin ligases: new structures, new insights, new questions. Biochem J 458: 421-437
    • (2014) Biochem J , vol.458 , pp. 421-437
    • Spratt, D.E.1    Walden, H.2    Shaw, G.S.3
  • 40
    • 3943074512 scopus 로고    scopus 로고
    • Nuclear magnetic resonance spectro-scopy of high-molecular-weight proteins
    • Tugarinov V, Hwang PM, Kay LE, (2004) Nuclear magnetic resonance spectro-scopy of high-molecular-weight proteins. Annu Rev Biochem 73: 107-146
    • (2004) Annu Rev Biochem , vol.73 , pp. 107-146
    • Tugarinov, V.1    Hwang, P.M.2    Kay, L.E.3
  • 42
    • 84881477223 scopus 로고    scopus 로고
    • Structure of the human Parkin ligase domain in an autoinhibited state
    • Wauer T, Komander D, (2013) Structure of the human Parkin ligase domain in an autoinhibited state. EMBO J 32: 2099-2112
    • (2013) EMBO J , vol.32 , pp. 2099-2112
    • Wauer, T.1    Komander, D.2
  • 43
    • 84939795423 scopus 로고    scopus 로고
    • Mechanism of phospho-ubiquitin-induced PARKIN activation
    • Wauer T, Simicek M, Schubert A, Komander D, (2015) Mechanism of phospho-ubiquitin-induced PARKIN activation. Nature 524: 370-374
    • (2015) Nature , vol.524 , pp. 370-374
    • Wauer, T.1    Simicek, M.2    Schubert, A.3    Komander, D.4
  • 44
    • 79957949190 scopus 로고    scopus 로고
    • UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids
    • Wenzel DM, Lissounov A, Brzovic PS, Klevit RE, (2011) UBCH7 reactivity profile reveals parkin and HHARI to be RING/HECT hybrids. Nature 474: 105-108
    • (2011) Nature , vol.474 , pp. 105-108
    • Wenzel, D.M.1    Lissounov, A.2    Brzovic, P.S.3    Klevit, R.E.4
  • 45
    • 0033032816 scopus 로고    scopus 로고
    • Improved 1HN-detected triple resonance TROSY-based experiments
    • Yang D, Kay LE, (1999) Improved 1HN-detected triple resonance TROSY-based experiments. J Biomol NMR 13: 3-10
    • (1999) J Biomol NMR , vol.13 , pp. 3-10
    • Yang, D.1    Kay, L.E.2
  • 46
    • 84879885169 scopus 로고    scopus 로고
    • Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism
    • Zheng X, Hunter T, (2013) Parkin mitochondrial translocation is achieved through a novel catalytic activity coupled mechanism. Cell Res 23: 886-897
    • (2013) Cell Res , vol.23 , pp. 886-897
    • Zheng, X.1    Hunter, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.