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Volumn 296, Issue 4, 2002, Pages 813-819

Identification of ubiquitin-like protein-binding subunits of the 26S proteasome

Author keywords

Dsk2; Proteasome; Rad23; Ubiquitin; Ubiquitin like domain

Indexed keywords

ADAPTOR PROTEIN; PROTEASOME; PROTEIN DSK2; PROTEIN RAD23; PROTEIN SUBUNIT; UBIQUITIN; UNCLASSIFIED DRUG;

EID: 0036382885     PISSN: 0006291X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0006-291X(02)02002-8     Document Type: Article
Times cited : (122)

References (27)
  • 2
    • 0032867676 scopus 로고    scopus 로고
    • The 26S proteasome: A molecular machine designed for controlled proteolysis
    • D. Voges, P. Zwickl, W. Baumeister, The 26S proteasome: a molecular machine designed for controlled proteolysis, Annu. Rev. Biochem. 68 (1999) 1015-1068.
    • (1999) Annu. Rev. Biochem. , vol.68 , pp. 1015-1068
    • Voges, D.1    Zwickl, P.2    Baumeister, W.3
  • 3
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • M.H. Glickman, A. Ciechanover, The ubiquitin-proteasome proteolytic pathway: destruction for the sake of construction, Physiol. Rev. 82 (2002) 373-428.
    • (2002) Physiol. Rev. , vol.82 , pp. 373-428
    • Glickman, M.H.1    Ciechanover, A.2
  • 4
    • 0032483546 scopus 로고    scopus 로고
    • A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3
    • M.H. Glickman, D.M. Rubin, O. Coux, I. Wefes, G. Pfeifer, Z. Cjeka, W. Baumeister, V.A. Fried, D. Finley, A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3, Cell 94 (1998) 615-623.
    • (1998) Cell , vol.94 , pp. 615-623
    • Glickman, M.H.1    Rubin, D.M.2    Coux, O.3    Wefes, I.4    Pfeifer, G.5    Cjeka, Z.6    Baumeister, W.7    Fried, V.A.8    Finley, D.9
  • 5
    • 0343081478 scopus 로고    scopus 로고
    • Rapid isolation and characterization of the yeast proteasome regulatory complex
    • Y. Saeki, A. Toh-e, H. Yokosawa, Rapid isolation and characterization of the yeast proteasome regulatory complex, Biochem. Biophys. Res. Commun. 273 (2000) 509-515.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 509-515
    • Saeki, Y.1    Toh-e, A.2    Yokosawa, H.3
  • 7
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
    • S. van Nocker, S. Sadis, D.M. Rubin, M. Glickman, H. Fu, O. Coux, I. Wefes, D. Finley, R.D. Vierstra, The multiubiquitin-chain-binding protein Mcb1 is a component of the 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover, Mol. Cell. Biol. 16 (1996) 6020-6028.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6020-6028
    • Van Nocker, S.1    Sadis, S.2    Rubin, D.M.3    Glickman, M.4    Fu, H.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.D.9
  • 9
    • 0034685806 scopus 로고    scopus 로고
    • Analysis of a gene encoding Rpn10 of the fission yeast proteasome reveals that the polyubiquitin-binding site of this subunit is essential when Rpn12/Mts3 activity is compromised
    • C.R.M. Wilkinson, K. Ferrell, M. Penney, M. Wallace, W. Dubiel, C. Gordon, Analysis of a gene encoding Rpn10 of the fission yeast proteasome reveals that the polyubiquitin-binding site of this subunit is essential when Rpn12/Mts3 activity is compromised, J. Biol. Chem. 275 (2000) 15182-15192.
    • (2000) J. Biol. Chem. , vol.275 , pp. 15182-15192
    • Wilkinson, C.R.M.1    Ferrell, K.2    Penney, M.3    Wallace, M.4    Dubiel, W.5    Gordon, C.6
  • 11
    • 0032879814 scopus 로고    scopus 로고
    • Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae
    • D. Lambertson, L. Chen, K. Madura, Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae, Genetics 153 (1999) 69-79.
    • (1999) Genetics , vol.153 , pp. 69-79
    • Lambertson, D.1    Chen, L.2    Madura, K.3
  • 15
    • 0036277299 scopus 로고    scopus 로고
    • Rad23 promotes the targeting of proteolytic substrates to the proteasome
    • L. Chen, K. Madura, Rad23 promotes the targeting of proteolytic substrates to the proteasome, Mol. Cell. Biol. 22 (2002) 4902-4913.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 4902-4913
    • Chen, L.1    Madura, K.2
  • 16
    • 0037154160 scopus 로고    scopus 로고
    • Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
    • M. Funakoshi, T. Sasaki, T. Nishimoto, H. Kobayashi, Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome, Proc. Natl. Acad. Sci. USA 99 (2002) 745-750.
    • (2002) Proc. Natl. Acad. Sci. USA , vol.99 , pp. 745-750
    • Funakoshi, M.1    Sasaki, T.2    Nishimoto, T.3    Kobayashi, H.4
  • 17
    • 0037023716 scopus 로고    scopus 로고
    • Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23
    • H. Rao, A. Sastry, Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the ubiquitin-associated domain proteins Dsk2 and Rad23, J. Biol. Chem. 277 (2002) 11691-11695.
    • (2002) J. Biol. Chem. , vol.277 , pp. 11691-11695
    • Rao, H.1    Sastry, A.2
  • 18
    • 0036295955 scopus 로고    scopus 로고
    • Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis
    • Y. Saeki, A. Saitoh, A. Toh-e, H. Yokosawa, Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin-dependent proteolysis, Biochem. Biophys. Res. Commun. 293 (2002) 986-992.
    • (2002) Biochem. Biophys. Res. Commun. , vol.293 , pp. 986-992
    • Saeki, Y.1    Saitoh, A.2    Toh-e, A.3    Yokosawa, H.4
  • 19
    • 0033791447 scopus 로고    scopus 로고
    • Proteasomal proteomics: Identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes
    • R. Verma, S. Chen, R. Feldman, D. Schieltz, J. Yates, J. Dohmen, R.J. Deshaies, Proteasomal proteomics: identification of nucleotide-sensitive proteasome-interacting proteins by mass spectrometric analysis of affinity-purified proteasomes, Mol. Biol. Cell 11 (2000) 3425-3439.
    • (2000) Mol. Biol. Cell , vol.11 , pp. 3425-3439
    • Verma, R.1    Chen, S.2    Feldman, R.3    Schieltz, D.4    Yates, J.5    Dohmen, J.6    Deshaies, R.J.7
  • 20
    • 0028070372 scopus 로고
    • Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins
    • M. Fujimuro, H. Sawada, H. Yokosawa, Production and characterization of monoclonal antibodies specific to multi-ubiquitin chains of polyubiquitinated proteins, FEBS Lett. 349 (1994) 173-180.
    • (1994) FEBS Lett. , vol.349 , pp. 173-180
    • Fujimuro, M.1    Sawada, H.2    Yokosawa, H.3
  • 21
  • 22
    • 0033603339 scopus 로고    scopus 로고
    • Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination
    • S. Kumar, A.L. Talis, P.M. Howley, Identification of HHR23A as a substrate for E6-associated protein-mediated ubiquitination, J. Biol. Chem. 274 (1999) 18785-18792.
    • (1999) J. Biol. Chem. , vol.274 , pp. 18785-18792
    • Kumar, S.1    Talis, A.L.2    Howley, P.M.3
  • 23
    • 0033600798 scopus 로고    scopus 로고
    • Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26S proteasome
    • H. Hiyama, M. Yokoi, C. Masutani, K. Sugasawa, T. Maekawa, K. Tanaka, J.H.J. Hoeijmakers, F. Hanaoka, Interaction of hHR23 with S5a. The ubiquitin-like domain of hHR23 mediates interaction with S5a subunit of 26S proteasome, J. Biol. Chem. 274 (1999) 28019-28025.
    • (1999) J. Biol. Chem. , vol.274 , pp. 28019-28025
    • Hiyama, H.1    Yokoi, M.2    Masutani, C.3    Sugasawa, K.4    Maekawa, T.5    Tanaka, K.6    Hoeijmakers, J.H.J.7    Hanaoka, F.8
  • 24
    • 0037126632 scopus 로고    scopus 로고
    • Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome
    • H. Fu, N. Reis, Y. Lee, M.H. Glickman, R.D. Vierstra, Subunit interaction maps for the regulatory particle of the 26S proteasome and the COP9 signalosome, EMBO J. 20 (2001) 7096-7107.
    • (2001) EMBO J. , vol.20 , pp. 7096-7107
    • Fu, H.1    Reis, N.2    Lee, Y.3    Glickman, M.H.4    Vierstra, R.D.5
  • 25
    • 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, 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
  • 26
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • Y.A. Lam, T.G. Lawson, M. Velayutham, J.L. Zweier, C.M. Pickart, A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal, Nature 416 (2002) 763-767.
    • (2002) Nature , vol.416 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweier, J.L.4    Pickart, C.M.5
  • 27
    • 0033972319 scopus 로고    scopus 로고
    • Mapping subunit contacts in the regulatory complex of the 26S proteasome. S2 and S5b form a tetramer with ATPase subunit S4 and S7
    • C. Gorbea, D. Taillandier, M. Rechsteiner, Mapping subunit contacts in the regulatory complex of the 26S proteasome. S2 and S5b form a tetramer with ATPase subunit S4 and S7, J. Biol. Chem. 275 (2000) 875-882.
    • (2000) J. Biol. Chem. , vol.275 , pp. 875-882
    • Gorbea, C.1    Taillandier, D.2    Rechsteiner, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.