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Volumn 21, Issue 2, 2011, Pages 257-264

Structural regulation of cullin-RING ubiquitin ligase complexes

Author keywords

[No Author keywords available]

Indexed keywords

CULLIN ASSOCIATED AND NEDDYLATION DISSOCIATED 1 PROTEIN; CULLIN RING LIGASE; LIGASE INHIBITOR; NEDD8 PROTEIN; UBIQUITIN PROTEIN LIGASE; UNCLASSIFIED DRUG;

EID: 79953068658     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.sbi.2011.01.003     Document Type: Review
Times cited : (167)

References (48)
  • 2
    • 33846497347 scopus 로고    scopus 로고
    • Regulation of catalytic activities of HECT ubiquitin ligases
    • Kee Y., Huibregtse J.M. Regulation of catalytic activities of HECT ubiquitin ligases. Biochem Biophys Res Commun 2007, 354:329-333.
    • (2007) Biochem Biophys Res Commun , vol.354 , pp. 329-333
    • Kee, Y.1    Huibregtse, J.M.2
  • 3
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • Petroski M.D., Deshaies R.J. Function and regulation of cullin-RING ubiquitin ligases. Nat Rev Mol Cell Biol 2005, 6:9-20.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 4
    • 78649653568 scopus 로고    scopus 로고
    • Structural assembly of cullin-RING ubiquitin ligase complexes
    • Zimmerman E.S., Schulman B.A., Zheng N. Structural assembly of cullin-RING ubiquitin ligase complexes. Curr Opin Struct Biol 2010, 20:714-721.
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 714-721
    • Zimmerman, E.S.1    Schulman, B.A.2    Zheng, N.3
  • 6
    • 70450218366 scopus 로고    scopus 로고
    • Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates
    • Kleiger G., Saha A., Lewis S., Kuhlman B., Deshaies R.J. Rapid E2-E3 assembly and disassembly enable processive ubiquitylation of cullin-RING ubiquitin ligase substrates. Cell 2009, 139:957-968.
    • (2009) Cell , vol.139 , pp. 957-968
    • Kleiger, G.1    Saha, A.2    Lewis, S.3    Kuhlman, B.4    Deshaies, R.J.5
  • 7
    • 71449123070 scopus 로고    scopus 로고
    • Detection of sequential polyubiquitylation on a millisecond timescale
    • Pierce N.W., Kleiger G., Shan S.O., Deshaies R.J. Detection of sequential polyubiquitylation on a millisecond timescale. Nature 2009, 462:615-619.
    • (2009) Nature , vol.462 , pp. 615-619
    • Pierce, N.W.1    Kleiger, G.2    Shan, S.O.3    Deshaies, R.J.4
  • 8
    • 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 2000, 102:533-539.
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4
  • 10
    • 0037756787 scopus 로고    scopus 로고
    • Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase
    • Wu G., Xu G., Schulman B.A., Jeffrey P.D., Harper J.W., Pavletich N.P. Structure of a beta-TrCP1-Skp1-beta-catenin complex: destruction motif binding and lysine specificity of the SCF(beta-TrCP1) ubiquitin ligase. Mol Cell 2003, 11:1445-1456.
    • (2003) Mol Cell , vol.11 , pp. 1445-1456
    • Wu, G.1    Xu, G.2    Schulman, B.A.3    Jeffrey, P.D.4    Harper, J.W.5    Pavletich, N.P.6
  • 11
    • 0037462424 scopus 로고    scopus 로고
    • Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase
    • Orlicky S., Tang X., Willems A., Tyers M., Sicheri F. Structural basis for phosphodependent substrate selection and orientation by the SCFCdc4 ubiquitin ligase. Cell 2003, 112:243-256.
    • (2003) Cell , vol.112 , pp. 243-256
    • Orlicky, S.1    Tang, X.2    Willems, A.3    Tyers, M.4    Sicheri, F.5
  • 12
    • 50449108516 scopus 로고    scopus 로고
    • Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation
    • Duda D.M., Borg L.A., Scott D.C., Hunt H.W., Hammel M., Schulman B.A. Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation. Cell 2008, 134:995-1006.
    • (2008) Cell , vol.134 , pp. 995-1006
    • Duda, D.M.1    Borg, L.A.2    Scott, D.C.3    Hunt, H.W.4    Hammel, M.5    Schulman, B.A.6
  • 13
    • 53349121021 scopus 로고    scopus 로고
    • Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation
    • Saha A., Deshaies R.J. Multimodal activation of the ubiquitin ligase SCF by Nedd8 conjugation. Mol Cell 2008, 32:21-31.
    • (2008) Mol Cell , vol.32 , pp. 21-31
    • Saha, A.1    Deshaies, R.J.2
  • 14
    • 50449110781 scopus 로고    scopus 로고
    • Autoinhibitory regulation of SCF-mediated ubiquitination by human cullin 1's C-terminal tail
    • Yamoah K., Oashi T., Sarikas A., Gazdoiu S., Osman R., Pan Z.Q. Autoinhibitory regulation of SCF-mediated ubiquitination by human cullin 1's C-terminal tail. Proc Natl Acad Sci U S A 2008, 105:12230-12235.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 12230-12235
    • Yamoah, K.1    Oashi, T.2    Sarikas, A.3    Gazdoiu, S.4    Osman, R.5    Pan, Z.Q.6
  • 15
    • 77956296853 scopus 로고    scopus 로고
    • Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family
    • Cui J., Yao Q., Li S., Ding X., Lu Q., Mao H., Liu L., Zheng N., Chen S., Shao F. Glutamine deamidation and dysfunction of ubiquitin/NEDD8 induced by a bacterial effector family. Science 2010, 329:1215-1218.
    • (2010) Science , vol.329 , pp. 1215-1218
    • Cui, J.1    Yao, Q.2    Li, S.3    Ding, X.4    Lu, Q.5    Mao, H.6    Liu, L.7    Zheng, N.8    Chen, S.9    Shao, F.10
  • 19
  • 26
    • 58149191374 scopus 로고    scopus 로고
    • Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality
    • Sharon M., Mao H., Boeri Erba E., Stephens E., Zheng N., Robinson C.V. Symmetrical modularity of the COP9 signalosome complex suggests its multifunctionality. Structure 2009, 17:31-40.
    • (2009) Structure , vol.17 , pp. 31-40
    • Sharon, M.1    Mao, H.2    Boeri Erba, E.3    Stephens, E.4    Zheng, N.5    Robinson, C.V.6
  • 27
    • 77951639210 scopus 로고    scopus 로고
    • Structural insights into the COP9 signalosome and its common architecture with the 26S proteasome lid and eIF3
    • Enchev R.I., Schreiber A., Beuron F., Morris E.P. Structural insights into the COP9 signalosome and its common architecture with the 26S proteasome lid and eIF3. Structure 2010, 18:518-527.
    • (2010) Structure , vol.18 , pp. 518-527
    • Enchev, R.I.1    Schreiber, A.2    Beuron, F.3    Morris, E.P.4
  • 28
    • 0036929129 scopus 로고    scopus 로고
    • NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases
    • Liu J., Furukawa M., Matsumoto T., Xiong Y. NEDD8 modification of CUL1 dissociates p120(CAND1), an inhibitor of CUL1-SKP1 binding and SCF ligases. Mol Cell 2002, 10:1511-1518.
    • (2002) Mol Cell , vol.10 , pp. 1511-1518
    • Liu, J.1    Furukawa, M.2    Matsumoto, T.3    Xiong, Y.4
  • 30
    • 8344251662 scopus 로고    scopus 로고
    • Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases
    • Goldenberg S.J., Cascio T.C., Shumway S.D., Garbutt K.C., Liu J., Xiong Y., Zheng N. Structure of the Cand1-Cul1-Roc1 complex reveals regulatory mechanisms for the assembly of the multisubunit cullin-dependent ubiquitin ligases. Cell 2004, 119:517-528.
    • (2004) Cell , vol.119 , pp. 517-528
    • Goldenberg, S.J.1    Cascio, T.C.2    Shumway, S.D.3    Garbutt, K.C.4    Liu, J.5    Xiong, Y.6    Zheng, N.7
  • 31
    • 33646697347 scopus 로고    scopus 로고
    • The structure of SOCS3 reveals the basis of the extended SH2 domain function and identifies an unstructured insertion that regulates stability
    • Babon J.J., McManus E.J., Yao S., DeSouza D.P., Mielke L.A., Sprigg N.S., Willson T.A., Hilton D.J., Nicola N.A., Baca M., et al. The structure of SOCS3 reveals the basis of the extended SH2 domain function and identifies an unstructured insertion that regulates stability. Mol Cell 2006, 22:205-216.
    • (2006) Mol Cell , vol.22 , pp. 205-216
    • Babon, J.J.1    McManus, E.J.2    Yao, S.3    DeSouza, D.P.4    Mielke, L.A.5    Sprigg, N.S.6    Willson, T.A.7    Hilton, D.J.8    Nicola, N.A.9    Baca, M.10
  • 32
    • 0037035851 scopus 로고    scopus 로고
    • Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling
    • Min J.H., Yang H., Ivan M., Gertler F., Kaelin W.G., Pavletich N.P. Structure of an HIF-1alpha -pVHL complex: hydroxyproline recognition in signaling. Science 2002, 296:1886-1889.
    • (2002) Science , vol.296 , pp. 1886-1889
    • Min, J.H.1    Yang, H.2    Ivan, M.3    Gertler, F.4    Kaelin, W.G.5    Pavletich, N.P.6
  • 36
    • 34047249627 scopus 로고    scopus 로고
    • Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases
    • Hao B., Oehlmann S., Sowa M.E., Harper J.W., Pavletich N.P. Structure of a Fbw7-Skp1-cyclin E complex: multisite-phosphorylated substrate recognition by SCF ubiquitin ligases. Mol Cell 2007, 26:131-143.
    • (2007) Mol Cell , vol.26 , pp. 131-143
    • Hao, B.1    Oehlmann, S.2    Sowa, M.E.3    Harper, J.W.4    Pavletich, N.P.5
  • 39
    • 25844441096 scopus 로고    scopus 로고
    • Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase
    • Hao B., Zheng N., Schulman B.A., Wu G., Miller J.J., Pagano M., Pavletich N.P. Structural basis of the Cks1-dependent recognition of p27(Kip1) by the SCF(Skp2) ubiquitin ligase. Mol Cell 2005, 20:9-19.
    • (2005) Mol Cell , vol.20 , pp. 9-19
    • Hao, B.1    Zheng, N.2    Schulman, B.A.3    Wu, G.4    Miller, J.J.5    Pagano, M.6    Pavletich, N.P.7
  • 42
    • 57049155555 scopus 로고    scopus 로고
    • Gibberellin-induced DELLA recognition by the gibberellin receptor GID1
    • Murase K., Hirano Y., Sun T.P., Hakoshima T. Gibberellin-induced DELLA recognition by the gibberellin receptor GID1. Nature 2008, 456:459-463.
    • (2008) Nature , vol.456 , pp. 459-463
    • Murase, K.1    Hirano, Y.2    Sun, T.P.3    Hakoshima, T.4
  • 43
    • 44449108005 scopus 로고    scopus 로고
    • Small-molecule agonists and antagonists of F-box protein-substrate interactions in auxin perception and signaling
    • Hayashi K., Tan X., Zheng N., Hatate T., Kimura Y., Kepinski S., Nozaki H. Small-molecule agonists and antagonists of F-box protein-substrate interactions in auxin perception and signaling. Proc Natl Acad Sci U S A 2008, 105:5632-5637.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5632-5637
    • Hayashi, K.1    Tan, X.2    Zheng, N.3    Hatate, T.4    Kimura, Y.5    Kepinski, S.6    Nozaki, H.7
  • 45
    • 52649138958 scopus 로고    scopus 로고
    • UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover
    • Alexandru G., Graumann J., Smith G.T., Kolawa N.J., Fang R., Deshaies R.J. UBXD7 binds multiple ubiquitin ligases and implicates p97 in HIF1alpha turnover. Cell 2008, 134:804-816.
    • (2008) Cell , vol.134 , pp. 804-816
    • Alexandru, G.1    Graumann, J.2    Smith, G.T.3    Kolawa, N.J.4    Fang, R.5    Deshaies, R.J.6
  • 46
    • 0032827002 scopus 로고    scopus 로고
    • Regulatory mechanisms of cellular response to oxidative stress
    • Itoh K., Ishii T., Wakabayashi N., Yamamoto M. Regulatory mechanisms of cellular response to oxidative stress. Free Radic Res 1999, 31:319-324.
    • (1999) Free Radic Res , vol.31 , pp. 319-324
    • Itoh, K.1    Ishii, T.2    Wakabayashi, N.3    Yamamoto, M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.