메뉴 건너뛰기




Volumn 14, Issue 18, 2004, Pages

Protein degradation: Recognition of ubiquitinylated substrates

Author keywords

[No Author keywords available]

Indexed keywords

SACCHAROMYCETALES;

EID: 4544290828     PISSN: 09609822     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.cub.2004.09.012     Document Type: Review
Times cited : (34)

References (19)
  • 1
    • 0035293622 scopus 로고    scopus 로고
    • Protein regulation by monoubiquitin
    • Hicke L. Protein regulation by monoubiquitin. Nat. Rev. Mol. Cell Biol. 2:2001;195-201
    • (2001) Nat. Rev. Mol. Cell Biol. , vol.2 , pp. 195-201
    • Hicke, L.1
  • 2
    • 0036083396 scopus 로고    scopus 로고
    • The ubiquitin-proteasome proteolytic pathway: Destruction for the sake of construction
    • Glickman M.H., Ciechanover A. 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
  • 3
    • 3142566639 scopus 로고    scopus 로고
    • Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system
    • Verma R., Oania R., Graumann J., Deshaies R.J. Multiubiquitin chain receptors define a layer of substrate selectivity in the ubiquitin-proteasome system. Cell. 118:2004;99-110
    • (2004) Cell , vol.118 , pp. 99-110
    • Verma, R.1    Oania, R.2    Graumann, J.3    Deshaies, R.J.4
  • 6
    • 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
    • van Nocker S., Sadis S., Rubin D.M., Glickman M., Fu H., Coux O., Wefes I., Finley D., Vierstra R.D. 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
  • 7
    • 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
    • Wilkinson C.R., Ferrell K., Penney M., Wallace M., Dubiel W., Gordon C. 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.1    Ferrell, K.2    Penney, M.3    Wallace, M.4    Dubiel, W.5    Gordon, C.6
  • 8
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • Hofmann K., Bucher P. The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem. Sci. 21:1996;172-173
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 11
    • 0032879814 scopus 로고    scopus 로고
    • Pleiotropic defects caused by loss of the proteasome-interacting factors Rad23 and Rpn10 of Saccharomyces cerevisiae
    • Lambertson D., Chen L., Madura K. 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
  • 12
    • 0037154160 scopus 로고    scopus 로고
    • Budding yeast Dsk2p is a polyubiquitin-binding protein that can interact with the proteasome
    • Funakoshi M., Sasaki T., Nishimoto T., Kobayashi H. 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
  • 13
    • 0037023716 scopus 로고    scopus 로고
    • Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the UBA domain proteins Dsk2 and Rad23
    • Rao H., Sastry A. Recognition of specific ubiquitin conjugates is important for the proteolytic functions of the UBA 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
  • 14
    • 0036295955 scopus 로고    scopus 로고
    • Ubiquitin-like proteins and Rpn10 play cooperative roles in ubiquitin- dependent proteolysis
    • Saeki Y., Saitoh A., Toh-e A., Yokosawa H. 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
  • 15
    • 0036277299 scopus 로고    scopus 로고
    • Rad23 promotes the targeting of proteolytic substrates to the proteasome
    • Chen L., Madura K. 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
  • 17
    • 0037646406 scopus 로고    scopus 로고
    • Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains
    • Raasi S., Pickart C.M. Rad23 ubiquitin-associated domains (UBA) inhibit 26 S proteasome-catalyzed proteolysis by sequestering lysine 48-linked polyubiquitin chains. J. Biol. Chem. 278:2003;8951-8959
    • (2003) J. Biol. Chem. , vol.278 , pp. 8951-8959
    • Raasi, S.1    Pickart, C.M.2
  • 18
    • 0038487228 scopus 로고    scopus 로고
    • Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: Dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains
    • Ye Y., Meyer H.H., Rapoport T.A. Function of the p97-Ufd1-Npl4 complex in retrotranslocation from the ER to the cytosol: dual recognition of nonubiquitinated polypeptide segments and polyubiquitin chains. J. Cell Biol. 162:2003;71-84
    • (2003) J. Cell Biol. , vol.162 , pp. 71-84
    • Ye, Y.1    Meyer, H.H.2    Rapoport, T.A.3
  • 19
    • 4444320698 scopus 로고    scopus 로고
    • A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation
    • Medicherla B., Kostova Z., Schaefer A., Wolf D.H. A genomic screen identifies Dsk2p and Rad23p as essential components of ER-associated degradation. EMBO Rep. 5:2004;692-697
    • (2004) EMBO Rep. , vol.5 , pp. 692-697
    • Medicherla, B.1    Kostova, Z.2    Schaefer, A.3    Wolf, D.H.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.