메뉴 건너뛰기




Volumn 408, Issue 3, 2011, Pages 420-431

Modulation of K11-linkage formation by variable loop residues within UbcH5A

Author keywords

anaphase promoting complex; APC; polyUb; polyubiquitin; Ub; ubiquitin; wild type; WT

Indexed keywords

CYSTEINE; LYSINE; LYSINE 11; POLYUBIQUITIN; PROTEIN; UBCH5A; UBIQUITIN; UBIQUITIN CONJUGATING ENZYME; UBIQUITIN CONJUGATING ENZYME E1; UBIQUITIN CONJUGATING ENZYME E2; UBIQUITIN CONJUGATING ENZYME E3; UNCLASSIFIED DRUG;

EID: 79953846027     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2011.03.011     Document Type: Article
Times cited : (38)

References (35)
  • 1
    • 0034915764 scopus 로고    scopus 로고
    • Mechanisms underlying ubiquitination
    • DOI 10.1146/annurev.biochem.70.1.503
    • Pickart C.M. Mechanisms underlying ubiquitination Annu. Rev. Biochem. 70 2001 503 533 (Pubitemid 32663902)
    • (2001) Annual Review of Biochemistry , vol.70 , pp. 503-533
    • Pickart, C.M.1
  • 2
    • 44649101850 scopus 로고    scopus 로고
    • Atypical ubiquitin chains: New molecular signals. 'Protein Modifications: Beyond the Usual Suspects' Review Series
    • DOI 10.1038/embor.2008.93, PII EMBOR200893
    • Ikeda F., and Dikic I. Atypical ubiquitin chains: new molecular signals. 'Protein Modifications: Beyond the Usual Suspects' Review Series EMBO Rep. 9 2008 536 542 (Pubitemid 351772916)
    • (2008) EMBO Reports , vol.9 , Issue.6 , pp. 536-542
    • Ikeda, F.1    Dikic, I.2
  • 3
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • DOI 10.1016/j.cbpa.2004.09.009, PII S1367593104001413
    • Pickart C.M., and Fushman D. Polyubiquitin chains: polymeric protein signals Curr. Opin. Chem. Biol. 8 2004 610 616 (Pubitemid 39535722)
    • (2004) Current Opinion in Chemical Biology , vol.8 , Issue.6 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 4
    • 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 H.T., Kim K.P., Lledias F., Kisselev A.F., Scaglione K.M., and Skowyra D. 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 2007 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
  • 6
    • 67649227630 scopus 로고    scopus 로고
    • Polyubiquitination by HECT E3s and the determinants of chain type specificity
    • Kim H.C., and Huibregtse J.M. Polyubiquitination by HECT E3s and the determinants of chain type specificity Mol. Cell. Biol. 29 2009 3307 3318
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 3307-3318
    • Kim, H.C.1    Huibregtse, J.M.2
  • 7
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Ye Y., and Rape M. Building ubiquitin chains: E2 enzymes at work Nat. Rev. Mol. Cell. Biol. 10 2009 755 764
    • (2009) Nat. Rev. Mol. Cell. Biol. , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 8
    • 77955990685 scopus 로고    scopus 로고
    • Catalysis of lysine 48-specific ubiquitin chain assembly by residues in E2 and ubiquitin
    • Rodrigo-Brenni M.C., Foster S.A., and Morgan D.O. Catalysis of lysine 48-specific ubiquitin chain assembly by residues in E2 and ubiquitin Mol. Cell 39 2010 548 559
    • (2010) Mol. Cell , vol.39 , pp. 548-559
    • Rodrigo-Brenni, M.C.1    Foster, S.A.2    Morgan, D.O.3
  • 9
    • 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 M.D., and Deshaies R.J. Mechanism of lysine 48-linked ubiquitin-chain synthesis by the Cullin-RING ubiquitin-ligase complex SCF-Cdc34 Cell 123 2005 1107 1120 (Pubitemid 41785424)
    • (2005) Cell , vol.123 , Issue.6 , pp. 1107-1120
    • Petroski, M.D.1    Deshaies, R.J.2
  • 10
    • 77951989723 scopus 로고    scopus 로고
    • Molecular basis for lysine specificity in the yeast ubiquitin-conjugating enzyme Cdc34
    • Sadowski, M., Suryadinata, R., Lai, X., Heierhorst, J. & Sarcevic, B. Molecular basis for lysine specificity in the yeast ubiquitin-conjugating enzyme Cdc34. Mol. Cell. Biol. 30, 2316-2329.
    • Mol. Cell. Biol. , vol.30 , pp. 2316-2329
    • Sadowski, M.1    Suryadinata, R.2    Lai, X.3    Heierhorst, J.4    Sarcevic, B.5
  • 11
    • 33749506057 scopus 로고    scopus 로고
    • Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation
    • DOI 10.1038/nsmb1148, PII NSMB1148
    • Eddins M.J., Carlile C.M., Gomez K.M., Pickart C.M., and Wolberger C. Mms2-Ubc13 covalently bound to ubiquitin reveals the structural basis of linkage-specific polyubiquitin chain formation Nat. Struct. Mol. Biol. 13 2006 915 920 (Pubitemid 44527374)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.10 , pp. 915-920
    • Eddins, M.J.1    Carlile, C.M.2    Gomez, K.M.3    Pickart, C.M.4    Wolberger, C.5
  • 12
    • 33845628859 scopus 로고    scopus 로고
    • Ubiquitin transfer from the E2 perspective: Why is UbcH5 so promiscuous?
    • Brzovic P.S., and Klevit R.E. Ubiquitin transfer from the E2 perspective: why is UbcH5 so promiscuous? Cell Cycle 5 2006 2867 2873 (Pubitemid 44953937)
    • (2006) Cell Cycle , vol.5 , Issue.24 , pp. 2867-2873
    • Brzovic, P.S.1    Klevit, R.E.2
  • 14
    • 34447097834 scopus 로고    scopus 로고
    • Sequential E2s Drive Polyubiquitin Chain Assembly on APC Targets
    • DOI 10.1016/j.cell.2007.05.027, PII S0092867407006654
    • Rodrigo-Brenni M.C., and Morgan D.O. Sequential E2s drive polyubiquitin chain assembly on APC targets Cell 130 2007 127 139 (Pubitemid 47031321)
    • (2007) Cell , vol.130 , Issue.1 , pp. 127-139
    • Rodrigo-Brenni, M.C.1    Morgan, D.O.2
  • 15
    • 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., and Klevit R.E. A UbcH5/ubiquitin noncovalent complex is required for processive BRCA1-directed ubiquitination Mol. Cell 21 2006 873 880 (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
  • 16
    • 73449088337 scopus 로고    scopus 로고
    • Crystal structure of UbcH5b~ubiquitin intermediate: Insight into the formation of the self-assembled E2~Ub conjugates
    • Sakata E., Satoh T., Yamamoto S., Yamaguchi Y., Yagi-Utsumi M., and Kurimoto E. Crystal structure of UbcH5b~ubiquitin intermediate: insight into the formation of the self-assembled E2~Ub conjugates Structure 18 2010 138 147
    • (2010) Structure , vol.18 , pp. 138-147
    • Sakata, E.1    Satoh, T.2    Yamamoto, S.3    Yamaguchi, Y.4    Yagi-Utsumi, M.5    Kurimoto, E.6
  • 18
    • 49549117842 scopus 로고    scopus 로고
    • Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies
    • Newton K., Matsumoto M.L., Wertz I.E., Kirkpatrick D.S., Lill J.R., and Tan J. Ubiquitin chain editing revealed by polyubiquitin linkage-specific antibodies Cell 134 2008 668 678
    • (2008) Cell , vol.134 , pp. 668-678
    • Newton, K.1    Matsumoto, M.L.2    Wertz, I.E.3    Kirkpatrick, D.S.4    Lill, J.R.5    Tan, J.6
  • 19
    • 33751515474 scopus 로고    scopus 로고
    • The Polycomb Protein Ring1B Generates Self Atypical Mixed Ubiquitin Chains Required for Its In Vitro Histone H2A Ligase Activity
    • DOI 10.1016/j.molcel.2006.10.022, PII S1097276506007283
    • Ben-Saadon R., Zaaroor D., Ziv T., and Ciechanover A. The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity Mol. Cell 24 2006 701 711 (Pubitemid 44839211)
    • (2006) Molecular Cell , vol.24 , Issue.5 , pp. 701-711
    • Ben-Saadon, R.1    Zaaroor, D.2    Ziv, T.3    Ciechanover, A.4
  • 20
    • 78649292467 scopus 로고    scopus 로고
    • Ubiquitin binding to A20 ZnF4 is required for modulation of NF-κB signaling
    • Bosanac I., Wertz I.E., Pan B., Yu C., Kusam S., and Lam C. Ubiquitin binding to A20 ZnF4 is required for modulation of NF-κB signaling Mol. Cell 40 2010 548 557
    • (2010) Mol. Cell , vol.40 , pp. 548-557
    • Bosanac, I.1    Wertz, I.E.2    Pan, B.3    Yu, C.4    Kusam, S.5    Lam, C.6
  • 21
    • 34248176792 scopus 로고    scopus 로고
    • Structure and Analysis of a Complex between SUMO and Ubc9 Illustrates Features of a Conserved E2-Ubl Interaction
    • DOI 10.1016/j.jmb.2007.04.006, PII S0022283607004603
    • Capili A.D., and Lima C.D. Structure and analysis of a complex between SUMO and Ubc9 illustrates features of a conserved E2-Ubl interaction J. Mol. Biol. 369 2007 608 618 (Pubitemid 46709931)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.3 , pp. 608-618
    • Capili, A.D.1    Lima, C.D.2
  • 22
    • 34248146499 scopus 로고    scopus 로고
    • Structure of a SUMO-binding-motif Mimic Bound to Smt3p-Ubc9p: Conservation of a Non-covalent Ubiquitin-like Protein-E2 Complex as a Platform for Selective Interactions within a SUMO Pathway
    • DOI 10.1016/j.jmb.2007.04.007, PII S0022283607004615
    • Duda D.M., van Waardenburg R.C., Borg L.A., McGarity S., Nourse A., and Waddell M.B. Structure of a SUMO-binding-motif mimic bound to Smt3p-Ubc9p: conservation of a non-covalent ubiquitin-like protein-E2 complex as a platform for selective interactions within a SUMO pathway J. Mol. Biol. 369 2007 619 630 (Pubitemid 46709932)
    • (2007) Journal of Molecular Biology , vol.369 , Issue.3 , pp. 619-630
    • Duda, D.M.1    Van Waardenburg, R.C.A.M.2    Borg, L.A.3    McGarity, S.4    Nourse, A.5    Waddell, M.B.6    Bjornsti, M.-A.7    Schulman, B.A.8
  • 23
    • 34250013122 scopus 로고    scopus 로고
    • Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation
    • DOI 10.1038/sj.emboj.7601711, PII 7601711
    • Knipscheer P., van Dijk W.J., Olsen J.V., Mann M., and Sixma T.K. Noncovalent interaction between Ubc9 and SUMO promotes SUMO chain formation EMBO J. 26 2007 2797 2807 (Pubitemid 46884280)
    • (2007) EMBO Journal , vol.26 , Issue.11 , pp. 2797-2807
    • Knipscheer, P.1    Van Dijk, W.J.2    Olsen, J.V.3    Mann, M.4    Sixma, T.K.5
  • 24
    • 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., and Rape M. Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex Cell 133 2008 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
  • 25
    • 20444384040 scopus 로고    scopus 로고
    • Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex
    • DOI 10.1038/nature03588
    • Reverter D., and Lima C.D. Insights into E3 ligase activity revealed by a SUMO-RanGAP1-Ubc9-Nup358 complex Nature 435 2005 687 692 (Pubitemid 40825514)
    • (2005) Nature , vol.435 , Issue.7042 , pp. 687-692
    • Reverter, D.1    Lima, C.D.2
  • 26
    • 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., and Lima C.D. Lysine activation and functional analysis of E2-mediated conjugation in the SUMO pathway Nat. Struct. Mol. Biol. 13 2006 491 499 (Pubitemid 43848903)
    • (2006) Nature Structural and Molecular Biology , vol.13 , Issue.6 , pp. 491-499
    • Yunus, A.A.1    Lima, C.D.2
  • 30
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu P., Duong D.M., Seyfried N.T., Cheng D., Xie Y., and Robert J. Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation Cell 137 2009 133 145
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4    Xie, Y.5    Robert, J.6
  • 31
    • 34250375116 scopus 로고    scopus 로고
    • E3-Independent Monoubiquitination of Ubiquitin-Binding Proteins
    • DOI 10.1016/j.molcel.2007.05.014, PII S1097276507003152
    • Hoeller D., Hecker C.M., Wagner S., Rogov V., Dotsch V., and Dikic I. E3-independent monoubiquitination of ubiquitin-binding proteins Mol. Cell 26 2007 891 898 (Pubitemid 46921003)
    • (2007) Molecular Cell , vol.26 , Issue.6 , pp. 891-898
    • Hoeller, D.1    Hecker, C.-M.2    Wagner, S.3    Rogov, V.4    Dotsch, V.5    Dikic, I.6
  • 33
    • 31044453144 scopus 로고    scopus 로고
    • The Evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor Emi1
    • DOI 10.1016/j.cell.2005.10.038, PII S0092867405013231
    • Eldridge A.G., Loktev A.V., Hansen D.V., Verschuren E.W., Reimann J.D., and Jackson P.K. The evi5 oncogene regulates cyclin accumulation by stabilizing the anaphase-promoting complex inhibitor emi1 Cell 124 2006 367 380 (Pubitemid 43121984)
    • (2006) Cell , vol.124 , Issue.2 , pp. 367-380
    • Eldridge, A.G.1    Loktev, A.V.2    Hansen, D.V.3    Verschuren, E.W.4    Reimann, J.D.R.5    Jackson, P.K.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.