메뉴 건너뛰기




Volumn 12, Issue 4, 2011, Pages 342-349

Structure of the HECT:ubiquitin complex and its role in ubiquitin chain elongation

Author keywords

catalysis; E3 ligase; polyubiquitination; structure; ubiquitin

Indexed keywords

CYSTEINE; UBIQUITIN; UBIQUITIN PROTEIN LIGASE HECT; UBIQUITIN PROTEIN LIGASE NEDD4; UNCLASSIFIED DRUG;

EID: 79953325889     PISSN: 1469221X     EISSN: 14693178     Source Type: Journal    
DOI: 10.1038/embor.2011.21     Document Type: Article
Times cited : (140)

References (23)
  • 1
    • 76449098262 scopus 로고    scopus 로고
    • PHENIX: A comprehensive Python-based system for macromolecular structure solution
    • Adams PD et al (2010) PHENIX: a comprehensive Python-based system for macromolecular structure solution. Acta Crystallogr D Biol Crystallogr 66: 213-221
    • (2010) Acta Crystallogr D Biol Crystallogr , vol.66 , pp. 213-221
    • Adams, P.D.1
  • 2
    • 37049014272 scopus 로고    scopus 로고
    • Version 1.2 of the Crystallography and NMR system
    • Brunger AT (2007) Version 1.2 of the Crystallography and NMR system. Nat Protoc 2: 2728-2733
    • (2007) Nat Protoc , vol.2 , pp. 2728-2733
    • Brunger, A.T.1
  • 3
    • 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
  • 4
    • 34347265174 scopus 로고    scopus 로고
    • Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins
    • DOI 10.1146/annurev.biophys.36.040306.132820
    • Dye BT, Schulman BA (2007) Structural mechanisms underlying posttranslational modification by ubiquitin-like proteins. Annu Rev Biophys Biomol Struct 36: 131-150 (Pubitemid 46998113)
    • (2007) Annual Review of Biophysics and Biomolecular Structure , vol.36 , pp. 131-150
    • Dye, B.T.1    Schulman, B.A.2
  • 6
    • 66449125689 scopus 로고    scopus 로고
    • Regulation of the RSP5 ubiquitin ligase by an intrinsic ubiquitin-binding site
    • French ME, Kretzmann BR, Hicke L (2009) Regulation of the RSP5 ubiquitin ligase by an intrinsic ubiquitin-binding site. J Biol Chem 284: 12071-12079
    • (2009) J Biol Chem , vol.284 , pp. 12071-12079
    • French, M.E.1    Kretzmann, B.R.2    Hicke, L.3
  • 7
    • 30344482590 scopus 로고    scopus 로고
    • Lingering mysteries of ubiquitin-chain assembly
    • DOI 10.1016/j.cell.2005.12.025, PII S0092867405014662
    • Hochstrasser M (2006) Lingering mysteries of ubiquitin-chain assembly. Cell 124: 27-34 (Pubitemid 43069307)
    • (2006) Cell , vol.124 , Issue.1 , pp. 27-34
    • Hochstrasser, M.1
  • 9
    • 43049162227 scopus 로고    scopus 로고
    • Mechanism of Ubiquitin-Chain Formation by the Human Anaphase-Promoting Complex
    • DOI 10.1016/j.cell.2008.04.012, PII S0092867408005035
    • Jin L, Williamson A, Banerjee S, Philipp I, Rape M (2008) Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex. Cell 133: 653-665 (Pubitemid 351636306)
    • (2008) Cell , vol.133 , Issue.4 , pp. 653-665
    • Jin, L.1    Williamson, A.2    Banerjee, S.3    Philipp, I.4    Rape, M.5
  • 12
    • 67649227630 scopus 로고    scopus 로고
    • Polyubiquitination by HECT E3s and the determinants of chain type specificity
    • Kim HC, Huibregtse JM (2009) Polyubiquitination by HECT E3s and the determinants of chain type specificity. Mol Cell Biol 29: 3307-3318
    • (2009) Mol Cell Biol , vol.29 , pp. 3307-3318
    • Kim, H.C.1    Huibregtse, J.M.2
  • 13
    • 34547130325 scopus 로고    scopus 로고
    • Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages
    • DOI 10.1074/jbc.M609659200
    • Kim HT, Kim KP, Lledias F, Kisselev AF, Scaglione KM, Skowyra D, Gygi SP, Goldberg AL (2007) Certain pairs of ubiquitin-conjugating enzymes (E2s) and ubiquitin-protein ligases (E3s) synthesize nondegradable forked ubiquitin chains containing all possible isopeptide linkages. J Biol Chem 282: 17375-17386 (Pubitemid 47100279)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.24 , pp. 17375-17386
    • Hyoung, T.K.1    Kwang, P.K.2    Lledias, F.3    Kisselev, A.F.4    Scaglione, K.M.5    Skowyra, D.6    Gygi, S.P.7    Goldberg, A.L.8
  • 15
    • 34548232365 scopus 로고    scopus 로고
    • Inference of Macromolecular Assemblies from Crystalline State
    • DOI 10.1016/j.jmb.2007.05.022, PII S0022283607006420
    • Krissinel E, Henrick K (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797 (Pubitemid 47321791)
    • (2007) Journal of Molecular Biology , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 18
    • 77949888615 scopus 로고    scopus 로고
    • The ubiquitin binding region of the Smurf HECT domain facilitates polyubiquitylation and binding of ubiquitylated substrates
    • Ogunjimi AA, Wiesner S, Briant DJ, Varelas X, Sicheri F, Forman-Kay J, Wrana JL (2010) The ubiquitin binding region of the Smurf HECT domain facilitates polyubiquitylation and binding of ubiquitylated substrates. J Biol Chem 285: 6308-6315
    • (2010) J Biol Chem , vol.285 , pp. 6308-6315
    • Ogunjimi, A.A.1    Wiesner, S.2    Briant, D.J.3    Varelas, X.4    Sicheri, F.5    Forman-Kay, J.6    Wrana, J.L.7
  • 19
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • DOI 10.1016/S0076-6879(97)76066-X
    • Otwinowski Z, Minor W (1997) Processing of X-ray diffraction data collected in oscillation mode. Methods Enzymol 276: 307-326 (Pubitemid 27085611)
    • (1997) Methods in Enzymology , vol.276 , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 20
    • 28944435024 scopus 로고    scopus 로고
    • Mechanism of lysine 48-linked ubiquitin-chain synthesis by the cullin-RING ubiquitin-ligase complex SCF-Cdc34
    • DOI 10.1016/j.cell.2005.09.033, PII S0092867405010391
    • Petroski MD, Deshaies RJ (2005) Mechanism of lysine 48-linked ubiquitin- chain synthesis by the cullin-RING ubiquitin-ligase complex SCF-Cdc34. Cell 123: 1107-1120 (Pubitemid 41785424)
    • (2005) Cell , vol.123 , Issue.6 , pp. 1107-1120
    • Petroski, M.D.1    Deshaies, R.J.2
  • 21
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • Rotin D, Kumar S (2009) Physiological functions of the HECT family of ubiquitin ligases. Nat RevMol Cell Biol 10: 398-409
    • (2009) Nat RevMol Cell Biol , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 22
    • 0037249354 scopus 로고    scopus 로고
    • Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase
    • DOI 10.1016/S1097-2765(02)00774-8
    • Verdecia MA, Joazeiro CA, Wells NJ, Ferrer JL, Bowman ME, Hunter T, Noel JP (2003) Conformational flexibility underlies ubiquitin ligation mediated by the WWP1 HECT domain E3 ligase. Mol Cell 11: 249-259 (Pubitemid 36126605)
    • (2003) Molecular Cell , vol.11 , Issue.1 , pp. 249-259
    • Verdecia, M.A.1    Joazeiro, C.A.P.2    Wells, N.J.3    Ferrer, J.-L.4    Bowman, M.E.5    Hunter, T.6    Noel, J.P.7
  • 23
    • 33646122226 scopus 로고    scopus 로고
    • Molecular determinants of polyubiquitin linkage selection by an HECT ubiquitin ligase
    • Wang M, Cheng D, Peng J, Pickart CM (2006) Molecular determinants of polyubiquitin linkage selection by an HECT ubiquitin ligase. EMBOJ25: 1710-1719
    • (2006) EMBOJ , vol.25 , pp. 1710-1719
    • Wang, M.1    Cheng, D.2    Peng, J.3    Pickart, C.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.