메뉴 건너뛰기




Volumn 21, Issue 5, 2013, Pages 727-740

Mixed-linkage ubiquitin chains send mixed messages

Author keywords

[No Author keywords available]

Indexed keywords

UBIQUITIN;

EID: 84877576390     PISSN: 09692126     EISSN: 18784186     Source Type: Journal    
DOI: 10.1016/j.str.2013.02.019     Document Type: Article
Times cited : (85)

References (33)
  • 1
    • 33751515474 scopus 로고    scopus 로고
    • The polycomb protein Ring1B generates self atypical mixed ubiquitin chains required for its in vitro histone H2A ligase activity
    • R. Ben-Saadon, D. Zaaroor, T. Ziv, and A. Ciechanover 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
    • (2006) Mol. Cell , vol.24 , pp. 701-711
    • Ben-Saadon, R.1    Zaaroor, D.2    Ziv, T.3    Ciechanover, A.4
  • 2
    • 62649104153 scopus 로고    scopus 로고
    • K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1
    • E.M. Cooper, C. Cutcliffe, T.Z. Kristiansen, A. Pandey, C.M. Pickart, and R.E. Cohen K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1 EMBO J. 28 2009 621 631
    • (2009) EMBO J. , vol.28 , pp. 621-631
    • Cooper, E.M.1    Cutcliffe, C.2    Kristiansen, T.Z.3    Pandey, A.4    Pickart, C.M.5    Cohen, R.E.6
  • 5
    • 77955391393 scopus 로고    scopus 로고
    • The HADDOCK web server for data-driven biomolecular docking
    • S.J. de Vries, M. van Dijk, and A.M. Bonvin The HADDOCK web server for data-driven biomolecular docking Nat. Protoc. 5 2010 883 897
    • (2010) Nat. Protoc. , vol.5 , pp. 883-897
    • De Vries, S.J.1    Van Dijk, M.2    Bonvin, A.M.3
  • 6
    • 82955193293 scopus 로고    scopus 로고
    • Structure and recognition of polyubiquitin chains of different lengths and linkage
    • D. Fushman, and K.D. Wilkinson Structure and recognition of polyubiquitin chains of different lengths and linkage F1000 Biol. Rep. 3 2011 26
    • (2011) F1000 Biol. Rep. , vol.3 , pp. 26
    • Fushman, D.1    Wilkinson, K.D.2
  • 7
    • 19344362846 scopus 로고    scopus 로고
    • The proteasome and the delicate balance between destruction and rescue
    • M.H. Glickman, and N. Adir The proteasome and the delicate balance between destruction and rescue PLoS Biol. 2 2004 E13
    • (2004) PLoS Biol. , vol.2 , pp. 13
    • Glickman, M.H.1    Adir, N.2
  • 9
    • 0025360747 scopus 로고
    • A uniform isopeptide-linked multiubiquitin chain is sufficient to target substrate for degradation in ubiquitin-mediated proteolysis
    • L. Gregori, M.S. Poosch, G. Cousins, and V. Chau A uniform isopeptide-linked multiubiquitin chain is sufficient to target substrate for degradation in ubiquitin-mediated proteolysis J. Biol. Chem. 265 1990 8354 8357
    • (1990) J. Biol. Chem. , vol.265 , pp. 8354-8357
    • Gregori, L.1    Poosch, M.S.2    Cousins, G.3    Chau, V.4
  • 11
    • 72149130935 scopus 로고    scopus 로고
    • The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome
    • A.D. Jacobson, N.Y. Zhang, P. Xu, K.J. Han, S. Noone, J. Peng, and C.W. Liu The lysine 48 and lysine 63 ubiquitin conjugates are processed differently by the 26 s proteasome J. Biol. Chem. 284 2009 35485 35494
    • (2009) J. Biol. Chem. , vol.284 , pp. 35485-35494
    • Jacobson, A.D.1    Zhang, N.Y.2    Xu, P.3    Han, K.J.4    Noone, S.5    Peng, J.6    Liu, C.W.7
  • 12
    • 84863266143 scopus 로고    scopus 로고
    • Formation of nondegradable forked ubiquitin conjugates by ring-finger ligases and its prevention by S5a
    • H.T. Kim, and A.L. Goldberg Formation of nondegradable forked ubiquitin conjugates by ring-finger ligases and its prevention by S5a Methods Mol. Biol. 832 2012 639 652
    • (2012) Methods Mol. Biol. , vol.832 , pp. 639-652
    • Kim, H.T.1    Goldberg, A.L.2
  • 13
    • 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
    • H.T. Kim, K.P. Kim, F. Lledias, A.F. Kisselev, K.M. Scaglione, D. Skowyra, S.P. Gygi, and A.L. Goldberg 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
    • (2007) J. Biol. Chem. , vol.282 , pp. 17375-17386
    • Kim, H.T.1    Kim, K.P.2    Lledias, F.3    Kisselev, A.F.4    Scaglione, K.M.5    Skowyra, D.6    Gygi, S.P.7    Goldberg, A.L.8
  • 14
    • 67650427174 scopus 로고    scopus 로고
    • S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains
    • H.T. Kim, K.P. Kim, T. Uchiki, S.P. Gygi, and A.L. Goldberg S5a promotes protein degradation by blocking synthesis of nondegradable forked ubiquitin chains EMBO J. 28 2009 1867 1877
    • (2009) EMBO J. , vol.28 , pp. 1867-1877
    • Kim, H.T.1    Kim, K.P.2    Uchiki, T.3    Gygi, S.P.4    Goldberg, A.L.5
  • 16
    • 84858146420 scopus 로고    scopus 로고
    • Non-canonical ubiquitin-based signals for proteasomal degradation
    • Y. Kravtsova-Ivantsiv, and A. Ciechanover Non-canonical ubiquitin-based signals for proteasomal degradation J. Cell Sci. 125 2012 539 548
    • (2012) J. Cell Sci. , vol.125 , pp. 539-548
    • Kravtsova-Ivantsiv, Y.1    Ciechanover, A.2
  • 17
    • 79955470830 scopus 로고    scopus 로고
    • Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes
    • 10.1074/mcp.R110.003871 R110.003871
    • M.J. Lee, B.H. Lee, J. Hanna, R.W. King, and D. Finley Trimming of ubiquitin chains by proteasome-associated deubiquitinating enzymes Mol. Cell. Proteomics 10 2011 10.1074/mcp.R110.003871 R110.003871
    • (2011) Mol. Cell. Proteomics , vol.10
    • Lee, M.J.1    Lee, B.H.2    Hanna, J.3    King, R.W.4    Finley, D.5
  • 18
    • 4143080425 scopus 로고    scopus 로고
    • AMSH is an endosome-associated ubiquitin isopeptidase
    • J. McCullough, M.J. Clague, and S. Urbé AMSH is an endosome-associated ubiquitin isopeptidase J. Cell Biol. 166 2004 487 492
    • (2004) J. Cell Biol. , vol.166 , pp. 487-492
    • McCullough, J.1    Clague, M.J.2    Urbé, S.3
  • 20
    • 8844237615 scopus 로고    scopus 로고
    • Polyubiquitin chains: Polymeric protein signals
    • C.M. Pickart, and D. Fushman Polyubiquitin chains: polymeric protein signals Curr. Opin. Chem. Biol. 8 2004 610 616
    • (2004) Curr. Opin. Chem. Biol. , vol.8 , pp. 610-616
    • Pickart, C.M.1    Fushman, D.2
  • 21
    • 33947411739 scopus 로고    scopus 로고
    • A model of interdomain mobility in a multidomain protein
    • Y.E. Ryabov, and D. Fushman A model of interdomain mobility in a multidomain protein J. Am. Chem. Soc. 129 2007 3315 3327
    • (2007) J. Am. Chem. Soc. , vol.129 , pp. 3315-3327
    • Ryabov, Y.E.1    Fushman, D.2
  • 22
    • 69149088033 scopus 로고    scopus 로고
    • Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by tandem UIMs of RAP80
    • Y. Sato, A. Yoshikawa, H. Mimura, M. Yamashita, A. Yamagata, and S. Fukai Structural basis for specific recognition of Lys 63-linked polyubiquitin chains by tandem UIMs of RAP80 EMBO J. 28 2009 2461 2468
    • (2009) EMBO J. , vol.28 , pp. 2461-2468
    • Sato, Y.1    Yoshikawa, A.2    Mimura, H.3    Yamashita, M.4    Yamagata, A.5    Fukai, S.6
  • 23
    • 77950658888 scopus 로고    scopus 로고
    • Multiplex SILAC analysis of a cellular TDP-43 proteinopathy model reveals protein inclusions associated with SUMOylation and diverse polyubiquitin chains
    • N.T. Seyfried, Y.M. Gozal, E.B. Dammer, Q. Xia, D.M. Duong, D. Cheng, J.J. Lah, A.I. Levey, and J. Peng Multiplex SILAC analysis of a cellular TDP-43 proteinopathy model reveals protein inclusions associated with SUMOylation and diverse polyubiquitin chains Mol. Cell. Proteomics 9 2010 705 718
    • (2010) Mol. Cell. Proteomics , vol.9 , pp. 705-718
    • Seyfried, N.T.1    Gozal, Y.M.2    Dammer, E.B.3    Xia, Q.4    Duong, D.M.5    Cheng, D.6    Lah, J.J.7    Levey, A.I.8    Peng, J.9
  • 24
    • 62549161305 scopus 로고    scopus 로고
    • Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of rap80
    • J.J. Sims, and R.E. Cohen Linkage-specific avidity defines the lysine 63-linked polyubiquitin-binding preference of rap80 Mol. Cell 33 2009 775 783
    • (2009) Mol. Cell , vol.33 , pp. 775-783
    • Sims, J.J.1    Cohen, R.E.2
  • 25
    • 84860319353 scopus 로고    scopus 로고
    • Forging isopeptide bonds using thiol-ene chemistry: Site-specific coupling of ubiquitin molecules for studying the activity of isopeptidases
    • E.M. Valkevich, R.G. Guenette, N.A. Sanchez, Y.C. Chen, Y. Ge, and E.R. Strieter Forging isopeptide bonds using thiol-ene chemistry: site-specific coupling of ubiquitin molecules for studying the activity of isopeptidases J. Am. Chem. Soc. 134 2012 6916 6919
    • (2012) J. Am. Chem. Soc. , vol.134 , pp. 6916-6919
    • Valkevich, E.M.1    Guenette, R.G.2    Sanchez, N.A.3    Chen, Y.C.4    Ge, Y.5    Strieter, E.R.6
  • 26
    • 0036922992 scopus 로고    scopus 로고
    • Structural properties of polyubiquitin chains in solution
    • R. Varadan, O. Walker, C. Pickart, and D. Fushman Structural properties of polyubiquitin chains in solution J. Mol. Biol. 324 2002 637 647
    • (2002) J. Mol. Biol. , vol.324 , pp. 637-647
    • Varadan, R.1    Walker, O.2    Pickart, C.3    Fushman, D.4
  • 27
    • 1342304089 scopus 로고    scopus 로고
    • Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling
    • R. Varadan, M. Assfalg, A. Haririnia, S. Raasi, C. Pickart, and D. Fushman Solution conformation of Lys63-linked di-ubiquitin chain provides clues to functional diversity of polyubiquitin signaling J. Biol. Chem. 279 2004 7055 7063
    • (2004) J. Biol. Chem. , vol.279 , pp. 7055-7063
    • Varadan, R.1    Assfalg, M.2    Haririnia, A.3    Raasi, S.4    Pickart, C.5    Fushman, D.6
  • 28
    • 28844440078 scopus 로고    scopus 로고
    • Using NMR spectroscopy to monitor ubiquitin chain conformation and interactions with ubiquitin-binding domains
    • R. Varadan, M. Assfalg, and D. Fushman Using NMR spectroscopy to monitor ubiquitin chain conformation and interactions with ubiquitin-binding domains Methods Enzymol 399 2005 177 192
    • (2005) Methods Enzymol , vol.399 , pp. 177-192
    • Varadan, R.1    Assfalg, M.2    Fushman, D.3
  • 29
    • 20444391345 scopus 로고    scopus 로고
    • Structural determinants for selective recognition of a Lys48-linked polyubiquitin chain by a UBA domain
    • R. Varadan, M. Assfalg, S. Raasi, C. Pickart, and D. Fushman Structural determinants for selective recognition of a Lys48-linked polyubiquitin chain by a UBA domain Mol. Cell 18 2005 687 698
    • (2005) Mol. Cell , vol.18 , pp. 687-698
    • Varadan, R.1    Assfalg, M.2    Raasi, S.3    Pickart, C.4    Fushman, D.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.