메뉴 건너뛰기




Volumn 20, Issue 4, 2005, Pages 525-538

Chaperoned ubiquitylation - Crystal structures of the CHIP U box E3 ubiquitin ligase and a CHIP-Ubc13-Uev1a complex

Author keywords

[No Author keywords available]

Indexed keywords

UBIQUITIN PROTEIN LIGASE;

EID: 27944495299     PISSN: 10972765     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molcel.2005.09.023     Document Type: Article
Times cited : (353)

References (47)
  • 1
    • 0037195907 scopus 로고    scopus 로고
    • Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome
    • S. Alberti, J. Demand, C. Esser, N. Emmerich, H. Schild, and J. Hohfeld Ubiquitylation of BAG-1 suggests a novel regulatory mechanism during the sorting of chaperone substrates to the proteasome J. Biol. Chem. 277 2002 45920 45927
    • (2002) J. Biol. Chem. , vol.277 , pp. 45920-45927
    • Alberti, S.1    Demand, J.2    Esser, C.3    Emmerich, N.4    Schild, H.5    Hohfeld, J.6
  • 2
    • 0033013126 scopus 로고    scopus 로고
    • Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions
    • C.A. Ballinger, P. Connell, Y. Wu, Z. Hu, L.J. Thompson, L.Y. Yin, and C. Patterson Identification of CHIP, a novel tetratricopeptide repeat-containing protein that interacts with heat shock proteins and negatively regulates chaperone functions Mol. Cell. Biol. 19 1999 4535 4545
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 4535-4545
    • Ballinger, C.A.1    Connell, P.2    Wu, Y.3    Hu, Z.4    Thompson, L.J.5    Yin, L.Y.6    Patterson, C.7
  • 5
    • 0028103275 scopus 로고
    • Programs for protein crystallography
    • CCP4 (Collaborative Computational Project, Number 4)
    • CCP4 (Collaborative Computational Project, Number 4) Programs for protein crystallography Acta Crystallogr. D Biol. Crystallogr. 50 1994 760 763
    • (1994) Acta Crystallogr. D Biol. Crystallogr. , vol.50 , pp. 760-763
  • 6
    • 0036187476 scopus 로고    scopus 로고
    • TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90
    • G. Chen, P. Cao, and D.V. Goeddel TNF-induced recruitment and activation of the IKK complex require Cdc37 and Hsp90 Mol. Cell 9 2002 401 410
    • (2002) Mol. Cell , vol.9 , pp. 401-410
    • Chen, G.1    Cao, P.2    Goeddel, D.V.3
  • 8
    • 0036629253 scopus 로고    scopus 로고
    • Protein quality control: U-box-containing E3 ubiquitin ligases join the fold
    • D.M. Cyr, J. Hohfeld, and C. Patterson Protein quality control: U-box-containing E3 ubiquitin ligases join the fold Trends Biochem. Sci. 27 2002 368 375
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 368-375
    • Cyr, D.M.1    Hohfeld, J.2    Patterson, C.3
  • 9
    • 0032473425 scopus 로고    scopus 로고
    • The structure of the tetratricopeptide repeats of protein phosphatase 5: Implications for TPR-mediated protein-protein interactions
    • A.K. Das, P.T.W. Cohen, and D. Barford The structure of the tetratricopeptide repeats of protein phosphatase 5: implications for TPR-mediated protein-protein interactions EMBO J. 17 1998 1192 1199
    • (1998) EMBO J. , vol.17 , pp. 1192-1199
    • Das, A.K.1    Cohen, P.T.W.2    Barford, D.3
  • 10
    • 0034644474 scopus 로고    scopus 로고
    • Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain
    • L. Deng, C. Wang, E. Spencer, L. Yang, A. Braun, J. You, C. Slaughter, C. Pickart, and Z.J. Chen Activation of the IkappaB kinase complex by TRAF6 requires a dimeric ubiquitin-conjugating enzyme complex and a unique polyubiquitin chain Cell 103 2000 351 361
    • (2000) Cell , vol.103 , pp. 351-361
    • Deng, L.1    Wang, C.2    Spencer, E.3    Yang, L.4    Braun, A.5    You, J.6    Slaughter, C.7    Pickart, C.8    Chen, Z.J.9
  • 11
    • 0037082158 scopus 로고    scopus 로고
    • High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
    • Y. Durocher, S. Perret, and A. Kamen High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells Nucleic Acids Res. 30 2002 E9
    • (2002) Nucleic Acids Res. , vol.30 , pp. 9
    • Durocher, Y.1    Perret, S.2    Kamen, A.3
  • 13
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • J.M. Galan, and R. Haguenauer-Tsapis Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein EMBO J. 16 1997 5847 5854
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.M.1    Haguenauer-Tsapis, R.2
  • 15
    • 5444239863 scopus 로고    scopus 로고
    • U-box protein carboxyl terminus of Hsc70-interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat Tau and is involved in neurodegeneration of tauopathy
    • S. Hatakeyama, M. Matsumoto, T. Kamura, M. Murayama, D.H. Chui, E. Planel, R. Takahashi, K.I. Nakayama, and A. Takashima U-box protein carboxyl terminus of Hsc70-interacting protein (CHIP) mediates poly-ubiquitylation preferentially on four-repeat Tau and is involved in neurodegeneration of tauopathy J. Neurochem. 91 2004 299 307
    • (2004) J. Neurochem. , vol.91 , pp. 299-307
    • Hatakeyama, S.1    Matsumoto, M.2    Kamura, T.3    Murayama, M.4    Chui, D.H.5    Planel, E.6    Takahashi, R.7    Nakayama, K.I.8    Takashima, A.9
  • 17
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • C. Hoege, B. Pfander, G.L. Moldovan, G. Pyrowolakis, and S. Jentsch RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO Nature 419 2002 135 141
    • (2002) Nature , vol.419 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 18
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • R.M. Hofmann, and C.M. Pickart Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair Cell 96 1999 645 653
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 19
    • 4043096960 scopus 로고    scopus 로고
    • Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans
    • T. Hoppe, G. Cassata, J.M. Barral, W. Springer, A.H. Hutagalung, H.F. Epstein, and R. Baumeister Regulation of the myosin-directed chaperone UNC-45 by a novel E3/E4-multiubiquitylation complex in C. elegans Cell 118 2004 337 349
    • (2004) Cell , vol.118 , pp. 337-349
    • Hoppe, T.1    Cassata, G.2    Barral, J.M.3    Springer, W.4    Hutagalung, A.H.5    Epstein, H.F.6    Baumeister, R.7
  • 20
    • 4744348809 scopus 로고    scopus 로고
    • Notch-induced E2A degradation requires CHIP and Hsc70 as novel facilitators of ubiquitination
    • Z. Huang, L. Nie, M. Xu, and X.H. Sun Notch-induced E2A degradation requires CHIP and Hsc70 as novel facilitators of ubiquitination Mol. Cell. Biol. 24 2004 8951 8962
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8951-8962
    • Huang, Z.1    Nie, L.2    Xu, M.3    Sun, X.H.4
  • 21
    • 0035900793 scopus 로고    scopus 로고
    • CHIP is a U-box-dependent E3 ubiquitin ligase: Identification of Hsc70 as a target for ubiquitylation
    • J. Jiang, C.A. Ballinger, Y. Wu, Q. Dai, D.M. Cyr, J. Hohfeld, and C. Patterson CHIP is a U-box-dependent E3 ubiquitin ligase: identification of Hsc70 as a target for ubiquitylation J. Biol. Chem. 276 2001 42938 42944
    • (2001) J. Biol. Chem. , vol.276 , pp. 42938-42944
    • Jiang, J.1    Ballinger, C.A.2    Wu, Y.3    Dai, Q.4    Cyr, D.M.5    Hohfeld, J.6    Patterson, C.7
  • 22
    • 1542782162 scopus 로고    scopus 로고
    • Chaperone-dependent regulation of endothelial nitric-oxide synthase intracellular trafficking by the co-chaperone/ubiquitin ligase CHIP
    • J. Jiang, D. Cyr, R.W. Babbitt, W.C. Sessa, and C. Patterson Chaperone-dependent regulation of endothelial nitric-oxide synthase intracellular trafficking by the co-chaperone/ubiquitin ligase CHIP J. Biol. Chem. 278 2003 49332 49341
    • (2003) J. Biol. Chem. , vol.278 , pp. 49332-49341
    • Jiang, J.1    Cyr, D.2    Babbitt, R.W.3    Sessa, W.C.4    Patterson, C.5
  • 23
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • T.A. Jones, J.-Y. Zou, S.W. Cowan, and M. Kjeldgaard Improved methods for building protein models in electron density maps and the location of errors in these models Acta Crystallogr. A47 1991 110 119
    • (1991) Acta Crystallogr. , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.-Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 24
    • 0004148514 scopus 로고
    • MRC Laboratory of Molecular Biology Cambridge, UK
    • A.G.W. Leslie MOSFLM Users Guide 1995 MRC Laboratory of Molecular Biology Cambridge, UK
    • (1995) MOSFLM Users Guide
    • Leslie, A.G.W.1
  • 25
    • 0347986662 scopus 로고    scopus 로고
    • CHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcription
    • L. Li, H. Xin, X. Xu, M. Huang, X. Zhang, Y. Chen, S. Zhang, X.Y. Fu, and Z. Chang CHIP mediates degradation of Smad proteins and potentially regulates Smad-induced transcription Mol. Cell. Biol. 24 2004 856 864
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 856-864
    • Li, L.1    Xin, H.2    Xu, X.3    Huang, M.4    Zhang, X.5    Chen, Y.6    Zhang, S.7    Fu, X.Y.8    Chang, Z.9
  • 26
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • G.C. Meacham, C. Patterson, W. Zhang, J.M. Younger, and D.M. Cyr The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation Nat. Cell Biol. 3 2001 100 105
    • (2001) Nat. Cell Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 28
    • 0035684430 scopus 로고    scopus 로고
    • CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein
    • S. Murata, Y. Minami, M. Minami, T. Chiba, and K. Tanaka CHIP is a chaperone-dependent E3 ligase that ubiquitylates unfolded protein EMBO Rep. 2 2001 1133 1138
    • (2001) EMBO Rep. , vol.2 , pp. 1133-1138
    • Murata, S.1    Minami, Y.2    Minami, M.3    Chiba, T.4    Tanaka, K.5
  • 29
    • 1642576077 scopus 로고    scopus 로고
    • Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity
    • R. Nikolay, T. Wiederkehr, W. Rist, G. Kramer, M.P. Mayer, and B. Bukau Dimerization of the human E3 ligase CHIP via a coiled-coil domain is essential for its activity J. Biol. Chem. 279 2004 2673 2678
    • (2004) J. Biol. Chem. , vol.279 , pp. 2673-2678
    • Nikolay, R.1    Wiederkehr, T.2    Rist, W.3    Kramer, G.4    Mayer, M.P.5    Bukau, B.6
  • 30
    • 2542579359 scopus 로고    scopus 로고
    • Getting into position: The catalytic mechanisms of protein ubiquitylation
    • L.A. Passmore, and D. Barford Getting into position: the catalytic mechanisms of protein ubiquitylation Biochem. J. 379 2004 513 525
    • (2004) Biochem. J. , vol.379 , pp. 513-525
    • Passmore, L.A.1    Barford, D.2
  • 32
    • 0033434080 scopus 로고    scopus 로고
    • Probability-based protein identification by searching sequence databases using mass spectrometry data
    • D.N. Perkins, D.J. Pappin, D.M. Creasy, and J.S. Cottrell Probability-based protein identification by searching sequence databases using mass spectrometry data Electrophoresis 20 1999 3551 3567
    • (1999) Electrophoresis , vol.20 , pp. 3551-3567
    • Perkins, D.N.1    Pappin, D.J.2    Creasy, D.M.3    Cottrell, J.S.4
  • 34
    • 9744227183 scopus 로고    scopus 로고
    • Ubiquitin: Structures, functions, mechanisms
    • C.M. Pickart, and M.J. Eddins Ubiquitin: structures, functions, mechanisms Biochim. Biophys. Acta 1695 2004 55 72
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 55-72
    • Pickart, C.M.1    Eddins, M.J.2
  • 35
    • 0034646511 scopus 로고    scopus 로고
    • Structure of TPR domain-peptide complexes: Critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine
    • C. Scheufler, A. Brinker, G. Bourenkov, S. Pegoraro, L. Moroder, H. Bartunik, F.U. Hartl, and I. Moarefi Structure of TPR domain-peptide complexes: critical elements in the assembly of the Hsp70-Hsp90 multichaperone machine Cell 101 2000 199 210
    • (2000) Cell , vol.101 , pp. 199-210
    • Scheufler, C.1    Brinker, A.2    Bourenkov, G.3    Pegoraro, S.4    Moroder, L.5    Bartunik, H.6    Hartl, F.U.7    Moarefi, I.8
  • 36
    • 0033568595 scopus 로고    scopus 로고
    • TNF-mediated activation of the stress-activated protein kinase pathway: TNF receptor-associated factor 2 recruits and activates germinal center kinase related
    • C.S. Shi, A. Leonardi, J. Kyriakis, U. Siebenlist, and J.H. Kehrl TNF-mediated activation of the stress-activated protein kinase pathway: TNF receptor-associated factor 2 recruits and activates germinal center kinase related J. Immunol. 163 1999 3279 3285
    • (1999) J. Immunol. , vol.163 , pp. 3279-3285
    • Shi, C.S.1    Leonardi, A.2    Kyriakis, J.3    Siebenlist, U.4    Kehrl, J.H.5
  • 37
    • 1042266624 scopus 로고    scopus 로고
    • CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival
    • H. Shimura, D. Schwartz, S.P. Gygi, and K.S. Kosik CHIP-Hsc70 complex ubiquitinates phosphorylated tau and enhances cell survival J. Biol. Chem. 279 2004 4869 4876
    • (2004) J. Biol. Chem. , vol.279 , pp. 4869-4876
    • Shimura, H.1    Schwartz, D.2    Gygi, S.P.3    Kosik, K.S.4
  • 38
    • 0034616943 scopus 로고    scopus 로고
    • Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain
    • J. Spence, R.R. Gali, G. Dittmar, F. Sherman, M. Karin, and D. Finley Cell cycle-regulated modification of the ribosome by a variant multiubiquitin chain Cell 102 2000 67 76
    • (2000) Cell , vol.102 , pp. 67-76
    • Spence, J.1    Gali, R.R.2    Dittmar, G.3    Sherman, F.4    Karin, M.5    Finley, D.6
  • 39
    • 2342477917 scopus 로고    scopus 로고
    • The novel functions of ubiquitination in signaling
    • L. Sun, and Z.J. Chan The novel functions of ubiquitination in signaling Curr. Opin. Cell Biol. 16 2004 119 126
    • (2004) Curr. Opin. Cell Biol. , vol.16 , pp. 119-126
    • Sun, L.1    Chan, Z.J.2
  • 40
    • 0035875079 scopus 로고    scopus 로고
    • Molecular insights into polyubiquitin chain assembly: Crystal structure of the Mms2/Ubc13 heterodimer
    • A.P. VanDemark, R.M. Hofmann, C. Tsui, C.M. Pickart, and C. Wolberger Molecular insights into polyubiquitin chain assembly: crystal structure of the Mms2/Ubc13 heterodimer Cell 105 2001 711 720
    • (2001) Cell , vol.105 , pp. 711-720
    • Vandemark, A.P.1    Hofmann, R.M.2    Tsui, C.3    Pickart, C.M.4    Wolberger, C.5
  • 42
    • 0037039327 scopus 로고    scopus 로고
    • Protein turnover: A CHIP programmed for proteolysis
    • T. Wiederkehr, B. Bukau, and A. Buchberger Protein turnover: a CHIP programmed for proteolysis Curr. Biol. 12 2002 R26 R28
    • (2002) Curr. Biol. , vol.12
    • Wiederkehr, T.1    Bukau, B.2    Buchberger, A.3
  • 44
    • 0036789884 scopus 로고    scopus 로고
    • Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu
    • W. Xu, M. Marcu, X. Yuan, E. Mimnaugh, C. Patterson, and L. Neckers Chaperone-dependent E3 ubiquitin ligase CHIP mediates a degradative pathway for c-ErbB2/Neu Proc. Natl. Acad. Sci. USA 99 2002 12847 12852
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 12847-12852
    • Xu, W.1    Marcu, M.2    Yuan, X.3    Mimnaugh, E.4    Patterson, C.5    Neckers, L.6
  • 45
    • 11244349206 scopus 로고    scopus 로고
    • A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase
    • J.M. Younger, H.Y. Ren, L. Chen, C.Y. Fan, A. Fields, C. Patterson, and D.M. Cyr A foldable CFTR{Delta}F508 biogenic intermediate accumulates upon inhibition of the Hsc70-CHIP E3 ubiquitin ligase J. Cell Biol. 167 2004 1075 1085
    • (2004) J. Cell Biol. , vol.167 , pp. 1075-1085
    • Younger, J.M.1    Ren, H.Y.2    Chen, L.3    Fan, C.Y.4    Fields, A.5    Patterson, C.6    Cyr, D.M.7
  • 46
    • 0034682718 scopus 로고    scopus 로고
    • Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases
    • N. Zheng, P. Wang, P.D. Jeffrey, and N.P. Pavletich Structure of a c-Cbl-UbcH7 complex: RING domain function in ubiquitin-protein ligases Cell 102 2000 533 539
    • (2000) Cell , vol.102 , pp. 533-539
    • Zheng, N.1    Wang, P.2    Jeffrey, P.D.3    Pavletich, N.P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.