메뉴 건너뛰기




Volumn 20, Issue 8, 2013, Pages 982-986

Essentiality of a non-RING element in priming donor ubiquitin for catalysis by a monomeric E3

Author keywords

[No Author keywords available]

Indexed keywords

RING FINGER PROTEIN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE E3;

EID: 84881478295     PISSN: 15459993     EISSN: 15459985     Source Type: Journal    
DOI: 10.1038/nsmb.2621     Document Type: Article
Times cited : (109)

References (45)
  • 1
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A. & Ciechanover, A. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61, 761-807 (1992).
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 2
    • 63649086487 scopus 로고    scopus 로고
    • Targeting the ubiquitin system in cancer therapy
    • Hoeller, D. & Dikic, I. Targeting the ubiquitin system in cancer therapy. Nature 458, 438-444 (2009).
    • (2009) Nature , vol.458 , pp. 438-444
    • Hoeller, D.1    Dikic, I.2
  • 3
    • 54249104026 scopus 로고    scopus 로고
    • The ubiquitin system, disease, and drug discovery
    • Petroski, M.D. The ubiquitin system, disease, and drug discovery. BMC Biochem. 9 (suppl. 1), S7 (2008).
    • (2008) BMC Biochem. , vol.9 , Issue.SUPPL. 1
    • Petroski, M.D.1
  • 6
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • Zheng, N., Wang, P., Jeffrey, P.D. & Pavletich, N.P. Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases. Cell 102, 533-539 (2000).
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 7
    • 1842607157 scopus 로고    scopus 로고
    • Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches
    • DOI 10.1016/j.str.2004.03.004, PII S096921260400084X
    • Dominguez, C. et al. Structural model of the UbcH5B/CNOT4 complex revealed by combining NMR, mutagenesis, and docking approaches. Structure 12, 633-644 (2004). (Pubitemid 38447166)
    • (2004) Structure , vol.12 , Issue.4 , pp. 633-644
    • Dominguez, C.1    Bonvin, A.M.J.J.2    Winkler, G.S.3    Van Schaik, F.M.A.4    Timmers, H.Th.M.5    Boelens, R.6
  • 8
    • 57649120782 scopus 로고    scopus 로고
    • Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment
    • Mace, P.D. et al. Structures of the cIAP2 RING domain reveal conformational changes associated with ubiquitin-conjugating enzyme (E2) recruitment. J. Biol. Chem. 283, 31633-31640 (2008).
    • (2008) J. Biol. Chem. , vol.283 , pp. 31633-31640
    • MacE, P.D.1
  • 9
    • 67349242723 scopus 로고    scopus 로고
    • E2 interaction and dimerization in the crystal structure of TRAF6
    • Yin, Q. et al. E2 interaction and dimerization in the crystal structure of TRAF6. Nat. Struct. Mol. Biol. 16, 658-666 (2009).
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 658-666
    • Yin, Q.1
  • 11
    • 84866858702 scopus 로고    scopus 로고
    • Structure of an E3:E2~Ub complex reveals an allosteric mechanism shared among RING/U-box ligases
    • Pruneda, J.N. et al. Structure of an E3:E2~Ub complex reveals an allosteric mechanism shared among RING/U-box ligases. Mol. Cell 47, 933-942 (2012).
    • (2012) Mol. Cell , vol.47 , pp. 933-942
    • Pruneda, J.N.1
  • 12
    • 84865781586 scopus 로고    scopus 로고
    • Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis
    • Plechanovová, A., Jaffray, E.G., Tatham, M.H., Naismith, J.H. & Hay, R.T. Structure of a RING E3 ligase and ubiquitin-loaded E2 primed for catalysis. Nature 489, 115-120 (2012).
    • (2012) Nature , vol.489 , pp. 115-120
    • Plechanovová, A.1    Jaffray, E.G.2    Tatham, M.H.3    Naismith, J.H.4    Hay, R.T.5
  • 13
    • 84866124869 scopus 로고    scopus 로고
    • BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer
    • Dou, H., Buetow, L., Sibbet, G.J., Cameron, K. & Huang, D.T. BIRC7-E2 ubiquitin conjugate structure reveals the mechanism of ubiquitin transfer by a RING dimer. Nat. Struct. Mol. Biol. 19, 876-883 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 876-883
    • Dou, H.1    Buetow, L.2    Sibbet, G.J.3    Cameron, K.4    Huang, D.T.5
  • 14
    • 79953296212 scopus 로고    scopus 로고
    • Essential role for ubiquitin-ubiquitin-conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate
    • Saha, A., Lewis, S., Kleiger, G., Kuhlman, B. & Deshaies, R.J. Essential role for ubiquitin-ubiquitin-conjugating enzyme interaction in ubiquitin discharge from Cdc34 to substrate. Mol. Cell 42, 75-83 (2011).
    • (2011) Mol. Cell , vol.42 , pp. 75-83
    • Saha, A.1    Lewis, S.2    Kleiger, G.3    Kuhlman, B.4    Deshaies, R.J.5
  • 15
    • 79952290609 scopus 로고    scopus 로고
    • The mechanism of linkage-specifc ubiquitin chain elongation by a single-subunit E2
    • Wickliffe, K.E., Lorenz, S., Wemmer, D.E., Kuriyan, J. & Rape, M. The mechanism of linkage-specifc ubiquitin chain elongation by a single-subunit E2. Cell 144, 769-781 (2011).
    • (2011) Cell , vol.144 , pp. 769-781
    • Wickliffe, K.E.1    Lorenz, S.2    Wemmer, D.E.3    Kuriyan, J.4    Rape, M.5
  • 16
    • 84869112362 scopus 로고    scopus 로고
    • Protein tyrosine kinase regulation by ubiquitination: Critical roles of Cbl-family ubiquitin ligases
    • Mohapatra, B. et al. Protein tyrosine kinase regulation by ubiquitination: critical roles of Cbl-family ubiquitin ligases. Biochim. Biophys. Acta 1833, 122-139 (2013).
    • (2013) Biochim. Biophys. Acta , vol.1833 , pp. 122-139
    • Mohapatra, B.1
  • 18
    • 14444276991 scopus 로고    scopus 로고
    • 292 negative regulatory phosphorylation site of ZAP-70
    • DOI 10.1074/jbc.272.52.33140
    • Lupher, M.L. Jr., Songyang, Z., Shoelson, S.E., Cantley, L.C. & Band, H. The Cbl phosphotyrosine-binding domain selects a D(N/D)XpY motif and binds to the Tyr292 negative regulatory phosphorylation site of ZAP-70. J. Biol. Chem. 272, 33140-33144 (1997). (Pubitemid 28023658)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.52 , pp. 33140-33144
    • Lupher Jr., M.L.1    Songyang, Z.2    Shoelson, S.E.3    Cantley, L.C.4    Band, H.5
  • 20
    • 3142618052 scopus 로고    scopus 로고
    • Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations
    • DOI 10.1074/jbc.M404114200
    • Kassenbrock, C.K. & Anderson, S.M. Regulation of ubiquitin protein ligase activity in c-Cbl by phosphorylation-induced conformational change and constitutive activation by tyrosine to glutamate point mutations. J. Biol. Chem. 279, 28017-28027 (2004). (Pubitemid 38900072)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.27 , pp. 28017-28027
    • Kassenbrock, C.K.1    Anderson, S.M.2
  • 21
    • 77954928407 scopus 로고    scopus 로고
    • The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating affnity for the ubiquitin-conjugating enzyme
    • Ryan, P.E., Sivadasan-Nair, N., Nau, M.M., Nicholas, S. & Lipkowitz, S. The N terminus of Cbl-c regulates ubiquitin ligase activity by modulating affnity for the ubiquitin-conjugating enzyme. J. Biol. Chem. 285, 23687-23698 (2010).
    • (2010) J. Biol. Chem. , vol.285 , pp. 23687-23698
    • Ryan, P.E.1    Sivadasan-Nair, N.2    Nau, M.M.3    Nicholas, S.4    Lipkowitz, S.5
  • 22
    • 84856708226 scopus 로고    scopus 로고
    • Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl
    • Dou, H. et al. Structural basis for autoinhibition and phosphorylation-dependent activation of c-Cbl. Nat. Struct. Mol. Biol. 19, 184-192 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 184-192
    • Dou, H.1
  • 23
    • 84855505031 scopus 로고    scopus 로고
    • Autoinhibition and phosphorylation-induced activation mechanisms of human cancer and autoimmune disease-related E3 protein Cbl-b
    • Kobashigawa, Y. et al. Autoinhibition and phosphorylation-induced activation mechanisms of human cancer and autoimmune disease-related E3 protein Cbl-b. Proc. Natl. Acad. Sci. USA 108, 20579-20584 (2011).
    • (2011) Proc. Natl. Acad. Sci. USA , vol.108 , pp. 20579-20584
    • Kobashigawa, Y.1
  • 24
    • 33644850903 scopus 로고    scopus 로고
    • A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination
    • DOI 10.1016/j.molcel.2006.02.008, PII S1097276506000906
    • Brzovic, P.S., Lissounov, A., Christensen, D.E., Hoyt, D.W. & Klevit, R.E.A. UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination. Mol. Cell 21, 873-880 (2006). (Pubitemid 43376136)
    • (2006) Molecular Cell , vol.21 , Issue.6 , pp. 873-880
    • Brzovic, P.S.1    Lissounov, A.2    Christensen, D.E.3    Hoyt, D.W.4    Klevit, R.E.5
  • 25
    • 0033522219 scopus 로고    scopus 로고
    • Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase
    • Meng, W., Sawasdikosol, S., Burakoff, S.J. & Eck, M.J. Structure of the amino-terminal domain of Cbl complexed to its binding site on ZAP-70 kinase. Nature 398, 84-90 (1999).
    • (1999) Nature , vol.398 , pp. 84-90
    • Meng, W.1    Sawasdikosol, S.2    Burakoff, S.J.3    Eck, M.J.4
  • 26
    • 40949140084 scopus 로고    scopus 로고
    • Structural basis for a novel intrapeptidyl H-bond and reverse binding of c-Cbl-TKB domain substrates
    • DOI 10.1038/emboj.2008.18, PII EMBOJ200818
    • Ng, C. et al. Structural basis for a novel intrapeptidyl H-bond and reverse binding of c-Cbl-TKB domain substrates. EMBO J. 27, 804-816 (2008). (Pubitemid 351506681)
    • (2008) EMBO Journal , vol.27 , Issue.5 , pp. 804-816
    • Ng, C.1    Jackson, R.A.2    Buschdorf, J.P.3    Sun, Q.4    Guy, G.R.5    Sivaraman, J.6
  • 27
    • 84856708042 scopus 로고    scopus 로고
    • Phosphorylation-dependent activity of the deubiquitinase DUBA
    • Huang, O.W. et al. Phosphorylation-dependent activity of the deubiquitinase DUBA. Nat. Struct. Mol. Biol. 19, 171-175 (2012).
    • (2012) Nat. Struct. Mol. Biol. , vol.19 , pp. 171-175
    • Huang, O.W.1
  • 28
    • 80052442072 scopus 로고    scopus 로고
    • Mechanism of ubiquitylation by dimeric RING ligase RNF4
    • Plechanovová, A. et al. Mechanism of ubiquitylation by dimeric RING ligase RNF4. Nat. Struct. Mol. Biol. 18, 1052-1059 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 1052-1059
    • Plechanovová, A.1
  • 29
    • 84874590707 scopus 로고    scopus 로고
    • Regulation of ubiquitin transfer by XIAP, a dimeric RING E3 ligase
    • Nakatani, Y. et al. Regulation of ubiquitin transfer by XIAP, a dimeric RING E3 ligase. Biochem. J. 450, 629-638 (2013).
    • (2013) Biochem. J. , vol.450 , pp. 629-638
    • Nakatani, Y.1
  • 30
    • 20444384040 scopus 로고    scopus 로고
    • Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex
    • DOI 10.1038/nature03588
    • Reverter, D. & Lima, C.D. Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex. Nature 435, 687-692 (2005). (Pubitemid 40825514)
    • (2005) Nature , vol.435 , Issue.7042 , pp. 687-692
    • Reverter, D.1    Lima, C.D.2
  • 31
    • 33744911377 scopus 로고    scopus 로고
    • Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway
    • DOI 10.1038/nsmb1104, PII N1104
    • Yunus, A.A. & Lima, C.D. Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway. Nat. Struct. Mol. Biol. 13, 491-499 (2006). (Pubitemid 43848903)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.6 , pp. 491-499
    • Yunus, A.A.1    Lima, C.D.2
  • 32
    • 79955759159 scopus 로고    scopus 로고
    • Smac mimetics activate the E3 ligase activity of cIAP1 protein by promoting RING domain dimerization
    • Feltham, R. et al. Smac mimetics activate the E3 ligase activity of cIAP1 protein by promoting RING domain dimerization. J. Biol. Chem. 286, 17015-17028 (2011).
    • (2011) J. Biol. Chem. , vol.286 , pp. 17015-17028
    • Feltham, R.1
  • 33
    • 33846193699 scopus 로고    scopus 로고
    • An essential function of the extreme C-terminus of MDM2 can be provided by MDMX
    • DOI 10.1038/sj.emboj.7601469, PII 7601469
    • Uldrijan, S., Pannekoek, W.J. & Vousden, K.H. An essential function of the extreme C-terminus of MDM2 can be provided by MDMX. EMBO J. 26, 102-112 (2007). (Pubitemid 46094703)
    • (2007) EMBO Journal , vol.26 , Issue.1 , pp. 102-112
    • Uldrijan, S.1    Pannekoek, W.-J.2    Vousden, K.H.3
  • 34
    • 69749124557 scopus 로고    scopus 로고
    • Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modifcation of PCNA
    • Yunus, A.A. & Lima, C.D. Structure of the Siz/PIAS SUMO E3 ligase Siz1 and determinants required for SUMO modifcation of PCNA. Mol. Cell 35, 669-682 (2009).
    • (2009) Mol. Cell , vol.35 , pp. 669-682
    • Yunus, A.A.1    Lima, C.D.2
  • 37
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: Conformational control of conjugation
    • Duda, D.M. et al. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell 134, 995-1006 (2008).
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1
  • 38
    • 79961029062 scopus 로고    scopus 로고
    • A RING E3-substrate complex poised for ubiquitin-like protein transfer: Structural insights into cullin-RING ligases
    • Calabrese, M.F. et al. A RING E3-substrate complex poised for ubiquitin-like protein transfer: structural insights into cullin-RING ligases. Nat. Struct. Mol. Biol. 18, 947-949 (2011).
    • (2011) Nat. Struct. Mol. Biol. , vol.18 , pp. 947-949
    • Calabrese, M.F.1
  • 39
    • 84861206557 scopus 로고    scopus 로고
    • Selective recruitment of an E2~ubiquitin complex by an E3 ubiquitin ligase
    • Spratt, D.E., Wu, K., Kovacev, J., Pan, Z.Q. & Shaw, G.S. Selective recruitment of an E2~ubiquitin complex by an E3 ubiquitin ligase. J. Biol. Chem. 287, 17374-17385 (2012).
    • (2012) J. Biol. Chem. , vol.287 , pp. 17374-17385
    • Spratt, D.E.1    Wu, K.2    Kovacev, J.3    Pan, Z.Q.4    Shaw, G.S.5
  • 40
    • 0037697382 scopus 로고    scopus 로고
    • Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer
    • DOI 10.1074/jbc.M303177200
    • Bohnsack, R.N. & Haas, A.L. Conservation in the mechanism of Nedd8 activation by the human AppBp1-Uba3 heterodimer. J. Biol. Chem. 278, 26823-26830 (2003). (Pubitemid 36876832)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.29 , pp. 26823-26830
    • Bohnsack, R.N.1    Haas, A.L.2
  • 42
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project.
    • Collaborative Computational Project. The CCP4 suite: programs for protein crystallography. Acta Crystallogr. D Biol. Crystallogr. 50, 760-763 (1994).
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.