메뉴 건너뛰기




Volumn 15, Issue 13, 2005, Pages 1217-1221

The zinc finger of the CSN-associated deubiquitinating enzyme USP15 is essential to rescue the E3 ligase Rbx1

Author keywords

[No Author keywords available]

Indexed keywords

1,10 PHENANTHROLINE; 1,10-PHENANTHROLINE; CA 15-3 ANTIGEN; CARRIER PROTEIN; COMPLEMENTARY DNA; COP9 SIGNALOSOME; MUC1 MUCIN PEPTIDE; MULTIPROTEIN COMPLEX; PEPTIDE FRAGMENT; PEPTIDE HYDROLASE; PHENANTHROLINE DERIVATIVE; POLYUBIQUITIN; PROTEINASE; RBX1 PROTEIN, HUMAN; UBIQUITIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN SPECIFIC PROTEASE; UBIQUITIN-SPECIFIC PROTEASE; ZINC FINGER PROTEIN;

EID: 21844464322     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2005.05.059     Document Type: Article
Times cited : (125)

References (24)
  • 2
    • 32644487282 scopus 로고    scopus 로고
    • The COP9 signalosome: Its possible role in the ubiquitin system
    • R.J. Mayer A.J. Ciechanover M. Rechsteiner WILEY-VCH Verlag GmbH and Company KGaA Weinheim, Germany
    • D. Bech-Otschir, B. Kapelari, and W. Dubiel The COP9 signalosome: Its possible role in the ubiquitin system R.J. Mayer A.J. Ciechanover M. Rechsteiner Ubiquitin and the Chemistry of Life, Volume 1 2005 WILEY-VCH Verlag GmbH and Company KGaA Weinheim, Germany 348 369
    • (2005) Ubiquitin and the Chemistry of Life, Volume 1 , pp. 348-369
    • Bech-Otschir, D.1    Kapelari, B.2    Dubiel, W.3
  • 5
    • 0037509945 scopus 로고    scopus 로고
    • Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p
    • C. Zhou, S. Wee, E. Rhee, M. Naumann, W. Dubiel, and D.A. Wolf Fission yeast COP9/signalosome suppresses cullin activity through recruitment of the deubiquitylating enzyme Ubp12p Mol. Cell 11 2003 927 938
    • (2003) Mol. Cell , vol.11 , pp. 927-938
    • Zhou, C.1    Wee, S.2    Rhee, E.3    Naumann, M.4    Dubiel, W.5    Wolf, D.A.6
  • 6
    • 0037509859 scopus 로고    scopus 로고
    • The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage
    • R. Groisman, J. Polanowska, I. Kuraoka, J. Sawada, M. Saijo, R. Drapkin, A.F. Kisselev, K. Tanaka, and Y. Nakatani The ubiquitin ligase activity in the DDB2 and CSA complexes is differentially regulated by the COP9 signalosome in response to DNA damage Cell 113 2003 357 367
    • (2003) Cell , vol.113 , pp. 357-367
    • Groisman, R.1    Polanowska, J.2    Kuraoka, I.3    Sawada, J.4    Saijo, M.5    Drapkin, R.6    Kisselev, A.F.7    Tanaka, K.8    Nakatani, Y.9
  • 7
    • 0038185375 scopus 로고    scopus 로고
    • Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms
    • C. Liu, K.A. Powell, K. Mundt, L. Wu, A.M. Carr, and T. Caspari Cop9/signalosome subunits and Pcu4 regulate ribonucleotide reductase by both checkpoint-dependent and -independent mechanisms Genes Dev. 17 2003 1130 1140
    • (2003) Genes Dev. , vol.17 , pp. 1130-1140
    • Liu, C.1    Powell, K.A.2    Mundt, K.3    Wu, L.4    Carr, A.M.5    Caspari, T.6
  • 9
    • 0037351609 scopus 로고    scopus 로고
    • Analysis of the mutational effects of the COP/DET/FUS loci on genome expression profiles reveals their overlapping yet not identical roles in regulating Arabidopsis seedling development
    • L. Ma, H. Zhao, and X.W. Deng Analysis of the mutational effects of the COP/DET/FUS loci on genome expression profiles reveals their overlapping yet not identical roles in regulating Arabidopsis seedling development Development 130 2003 969 981
    • (2003) Development , vol.130 , pp. 969-981
    • Ma, L.1    Zhao, H.2    Deng, X.W.3
  • 10
    • 13144305043 scopus 로고    scopus 로고
    • The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex
    • N. Wei, T. Tsuge, G. Serino, N. Dohmae, K. Takio, M. Matsui, and X.W. Deng The COP9 complex is conserved between plants and mammals and is related to the 26S proteasome regulatory complex Curr. Biol. 8 1998 919 922
    • (1998) Curr. Biol. , vol.8 , pp. 919-922
    • Wei, N.1    Tsuge, T.2    Serino, G.3    Dohmae, N.4    Takio, K.5    Matsui, M.6    Deng, X.W.7
  • 12
    • 0034725525 scopus 로고    scopus 로고
    • Electron microscopy and subunit-subunit interaction studies reveal a first architecture of COP9 signalosome
    • B. Kapelari, D. Bech-Otschir, R. Hegerl, R. Schade, R. Dumdey, and W. Dubiel Electron microscopy and subunit-subunit interaction studies reveal a first architecture of COP9 signalosome J. Mol. Biol. 300 2000 1169 1178
    • (2000) J. Mol. Biol. , vol.300 , pp. 1169-1178
    • Kapelari, B.1    Bech-Otschir, D.2    Hegerl, R.3    Schade, R.4    Dumdey, R.5    Dubiel, W.6
  • 13
    • 0038686677 scopus 로고    scopus 로고
    • Evidence for a physical association of the COP9 signalosome, the proteasome, and specific SCF E3 ligases in vivo
    • Z. Peng, Y. Shen, S. Feng, X. Wang, B.N. Chitteti, R.D. Vierstra, and X.W. Deng Evidence for a physical association of the COP9 signalosome, the proteasome, and specific SCF E3 ligases in vivo Curr. Biol. 13 2003 R504 R505
    • (2003) Curr. Biol. , vol.13
    • Peng, Z.1    Shen, Y.2    Feng, S.3    Wang, X.4    Chitteti, B.N.5    Vierstra, R.D.6    Deng, X.W.7
  • 15
    • 9644268864 scopus 로고    scopus 로고
    • Mechanism and function of deubiquitinating enzymes
    • A.Y. Amerik, and M. Hochstrasser Mechanism and function of deubiquitinating enzymes Biochim. Biophys. Acta 1695 2004 189 207
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 189-207
    • Amerik, A.Y.1    Hochstrasser, M.2
  • 16
    • 13944258080 scopus 로고    scopus 로고
    • The finger domain of the human deubiquitinating enzyme HAUSP is a zinc ribbon
    • S.S. Krishna, and N.V. Grishin The finger domain of the human deubiquitinating enzyme HAUSP is a zinc ribbon Cell Cycle 3 2004 1046 1049
    • (2004) Cell Cycle , vol.3 , pp. 1046-1049
    • Krishna, S.S.1    Grishin, N.V.2
  • 17
    • 4644352805 scopus 로고    scopus 로고
    • A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7
    • M. Canning, C. Boutell, J. Parkinson, and R.D. Everett A RING finger ubiquitin ligase is protected from autocatalyzed ubiquitination and degradation by binding to ubiquitin-specific protease USP7 J. Biol. Chem. 279 2004 38160 38168
    • (2004) J. Biol. Chem. , vol.279 , pp. 38160-38168
    • Canning, M.1    Boutell, C.2    Parkinson, J.3    Everett, R.D.4
  • 18
    • 11244351579 scopus 로고    scopus 로고
    • Function and regulation of cullin-RING ubiquitin ligases
    • M.D. Petroski, and R.J. Deshaies Function and regulation of cullin-RING ubiquitin ligases Nat. Rev. Mol. Cell Biol. 6 2005 9 20
    • (2005) Nat. Rev. Mol. Cell Biol. , vol.6 , pp. 9-20
    • Petroski, M.D.1    Deshaies, R.J.2
  • 19
    • 0141750416 scopus 로고    scopus 로고
    • BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases
    • R. Geyer, S. Wee, S. Anderson, J. Yates, and D.A. Wolf BTB/POZ domain proteins are putative substrate adaptors for cullin 3 ubiquitin ligases Mol. Cell 12 2003 783 790
    • (2003) Mol. Cell , vol.12 , pp. 783-790
    • Geyer, R.1    Wee, S.2    Anderson, S.3    Yates, J.4    Wolf, D.A.5
  • 20
    • 0141426637 scopus 로고    scopus 로고
    • COP9 signalosome: A multifunctional regulator of SCF and other cullin-based ubiquitin ligases
    • G.A. Cope, and R.J. Deshaies COP9 signalosome: A multifunctional regulator of SCF and other cullin-based ubiquitin ligases Cell 114 2003 663 671
    • (2003) Cell , vol.114 , pp. 663-671
    • Cope, G.A.1    Deshaies, R.J.2
  • 22
    • 0345099331 scopus 로고    scopus 로고
    • The COP9 signalosome: An assembly and maintenance platform for cullin ubiquitin ligases?
    • D.A. Wolf, C. Zhou, and S. Wee The COP9 signalosome: An assembly and maintenance platform for cullin ubiquitin ligases? Nat. Cell Biol. 5 2003 1029 1033
    • (2003) Nat. Cell Biol. , vol.5 , pp. 1029-1033
    • Wolf, D.A.1    Zhou, C.2    Wee, S.3
  • 23
    • 17344364820 scopus 로고    scopus 로고
    • CSN facilitates Cullin-RING ubiquitin ligase function by counteracting autocatalytic adapter instability
    • S. Wee, R.K. Geyer, T. Toda, and D.A. Wolf CSN facilitates Cullin-RING ubiquitin ligase function by counteracting autocatalytic adapter instability Nat. Cell Biol. 7 2005 387 391
    • (2005) Nat. Cell Biol. , vol.7 , pp. 387-391
    • Wee, S.1    Geyer, R.K.2    Toda, T.3    Wolf, D.A.4
  • 24
    • 0033581898 scopus 로고    scopus 로고
    • Association with cullin partners protects ROC proteins from proteasome-dependent degradation
    • T. Ohta, J.J. Michel, and Y. Xiong Association with cullin partners protects ROC proteins from proteasome-dependent degradation Oncogene 18 1999 6758 6766
    • (1999) Oncogene , vol.18 , pp. 6758-6766
    • Ohta, T.1    Michel, J.J.2    Xiong, Y.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.