메뉴 건너뛰기




Volumn 16, Issue 16, 1997, Pages 4826-4838

In vivo disassembly of free polyubiquitin chains by yeast Ubp14 modulates rates of protein degradation by the proteasome

Author keywords

Isopeptidase T; Proteasome; Ubiquitin; Upb 14; Yeast

Indexed keywords

FUNGAL PROTEIN; POLYUBIQUITIN; PROTEASOME; UBIQUITIN;

EID: 0030746105     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.16.4826     Document Type: Article
Times cited : (203)

References (42)
  • 1
    • 0028073188 scopus 로고
    • Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain
    • Arnason, T. and Ellison, M.J. (1994) Stress resistance in Saccharomyces cerevisiae is strongly correlated with assembly of a novel type of multiubiquitin chain. Mol. Cell. Biol., 14, 7876-7883.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7876-7883
    • Arnason, T.1    Ellison, M.J.2
  • 3
    • 0030028574 scopus 로고    scopus 로고
    • EPF and RAD6 are recognized by 26S proteasome subunit 5
    • EPF and RAD6 are recognized by 26S proteasome subunit 5. J. Biol. Chem., 271, 2823-2831.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2823-2831
    • Baboshina, O.V.1    Haas, A.L.2
  • 4
    • 0026457302 scopus 로고
    • Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family
    • Baker, R.T., Tobias, J.W. and Varshavsky, A. (1992) Ubiquitin-specific proteases of Saccharomyces cerevisiae. Cloning of UBP2 and UBP3, and functional analysis of the UBP gene family. J. Biol. Chem., 267, 23364-23375.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23364-23375
    • Baker, R.T.1    Tobias, J.W.2    Varshavsky, A.3
  • 6
    • 0030052841 scopus 로고    scopus 로고
    • Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting
    • Beal, R., Deveraux, Q., Xia, G., Rechsteiner, M. and Pickart, C. (1996) Surface hydrophobic residues of multiubiquitin chains essential for proteolytic targeting. Proc. Natl Acad. Sci. USA, 93, 861-866.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 861-866
    • Beal, R.1    Deveraux, Q.2    Xia, G.3    Rechsteiner, M.4    Pickart, C.5
  • 7
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V., Tobias, J.W., Bachmair, A., Marriott, D., Ecker, D.J., Gonda, D.K. and Varshavsky, A. (1989) A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein. Science, 243, 1576-1583.
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 8
    • 0028999726 scopus 로고
    • Biogenesis, structure, and function of the yeast 20S proteasome
    • Chen, P. and Hochstrasser, M. (1995) Biogenesis, structure, and function of the yeast 20S proteasome. EMBO J., 14, 2620-2630.
    • (1995) EMBO J. , vol.14 , pp. 2620-2630
    • Chen, P.1    Hochstrasser, M.2
  • 9
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor
    • Chen, P., Johnson, P. Sommer, T., Jentsch, S. and Hochstrasser, M. (1993) Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATα2 repressor. Cell, 74, 357-369.
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen, P.1    Johnson, P.2    Sommer, T.3    Jentsch, S.4    Hochstrasser, M.5
  • 10
    • 0025644201 scopus 로고
    • A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin
    • Chen, Z. and Pickart, C.M. (1990) A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin. J. Biol. Chem., 265, 21835-21842.
    • (1990) J. Biol. Chem. , vol.265 , pp. 21835-21842
    • Chen, Z.1    Pickart, C.M.2
  • 11
    • 0028018268 scopus 로고
    • The ubiquitin-proteasome proteolytic pathway
    • Ciechanover, A. (1994) The ubiquitin-proteasome proteolytic pathway. Cell, 79, 13-21.
    • (1994) Cell , vol.79 , pp. 13-21
    • Ciechanover, A.1
  • 12
    • 0028883820 scopus 로고
    • The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo
    • DeMarini, D.J., Papa, F.R., Swaminathan, S., Ursic, D., Rasmussen, T.P., Culbertson, M.R. and Hochstrasser, M. (1995) The yeast SEN3 gene encodes a regulatory subunit of the 26S proteasome complex required for ubiquitin-dependent protein degradation in vivo. Mol. Cell. Biol., 15, 6311-6321.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6311-6321
    • DeMarini, D.J.1    Papa, F.R.2    Swaminathan, S.3    Ursic, D.4    Rasmussen, T.P.5    Culbertson, M.R.6    Hochstrasser, M.7
  • 13
    • 0028235965 scopus 로고
    • A 26S protease subunit that binds ubiquitin conjugates
    • Deveraux, Q., Ustrell, V., Pickart, C. and Rechsteiner, M. (1994) A 26S protease subunit that binds ubiquitin conjugates. J. Biol. Chem., 269, 7059-7061.
    • (1994) J. Biol. Chem. , vol.269 , pp. 7059-7061
    • Deveraux, Q.1    Ustrell, V.2    Pickart, C.3    Rechsteiner, M.4
  • 14
    • 0025838227 scopus 로고
    • Epitope-tagged ubiquitin. A new probe for analyzing ubiquitin function
    • Ellison, M.J. and Hochstrasser, M. (1991) Epitope-tagged ubiquitin. A new probe for analyzing ubiquitin function. J. Biol. Chem., 266, 21150-21157.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21150-21157
    • Ellison, M.J.1    Hochstrasser, M.2
  • 15
    • 0028859849 scopus 로고
    • A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro
    • Falquet, L., Paquet, N., Frutiger, S., Hughes, G.J., Hoang-Van, K. and Jaton, J.C. (1995) A human de-ubiquitinating enzyme with both isopeptidase and peptidase activities in vitro. FEBS Lett., 359, 73-77.
    • (1995) FEBS Lett. , vol.359 , pp. 73-77
    • Falquet, L.1    Paquet, N.2    Frutiger, S.3    Hughes, G.J.4    Hoang-Van, K.5    Jaton, J.C.6
  • 16
    • 0013601039 scopus 로고
    • Immunochemical probes of ubiquitin pool dynamics
    • Rechsteiner, M. (ed.), Plenum Press, New York
    • Haas, A.L. (1988) Immunochemical probes of ubiquitin pool dynamics. In Rechsteiner, M. (ed.), Ubiquitin. Plenum Press, New York, pp. 173-206.
    • (1988) Ubiquitin , pp. 173-206
    • Haas, A.L.1
  • 17
    • 0026530899 scopus 로고
    • A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains - Role in protein degradation
    • Hadari, T., Warms, J.V.B., Rose, I.A. and Hershko, A. (1992) A ubiquitin C-terminal isopeptidase that acts on polyubiquitin chains - role in protein degradation. J. Biol. Chem., 267, 719-727.
    • (1992) J. Biol. Chem. , vol.267 , pp. 719-727
    • Hadari, T.1    Warms, J.V.B.2    Rose, I.A.3    Hershko, A.4
  • 19
    • 0028935165 scopus 로고
    • Ubiquitin, proteasomes, and the regulation of intracellular protein degradation
    • Hochstrasser, M. (1995) Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol., 7, 215-223.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 215-223
    • Hochstrasser, M.1
  • 20
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser, M. (1996) Ubiquitin-dependent protein degradation. Annu. Rev. Genet., 30, 405-439.
    • (1996) Annu. Rev. Genet. , vol.30 , pp. 405-439
    • Hochstrasser, M.1
  • 21
    • 0025331090 scopus 로고
    • In vivo degradation of a transcriptional regulator: The yeast α2 repressor
    • Hochstrasser, M. and Varshavsky, A. (1990) In vivo degradation of a transcriptional regulator: the yeast α2 repressor. Cell, 61, 697-708.
    • (1990) Cell , vol.61 , pp. 697-708
    • Hochstrasser, M.1    Varshavsky, A.2
  • 22
    • 0025853324 scopus 로고
    • The short-lived MATα2 transcriptional regulator is ubiquitinated in vivo
    • Hochstrasser, M., Ellison, M.J., Chau, V. and Varshavsky, A. (1991) The short-lived MATα2 transcriptional regulator is ubiquitinated in vivo. Proc. Natl Acad Sci. USA, 88, 4606-4610.
    • (1991) Proc. Natl Acad Sci. USA , vol.88 , pp. 4606-4610
    • Hochstrasser, M.1    Ellison, M.J.2    Chau, V.3    Varshavsky, A.4
  • 24
    • 85047669941 scopus 로고    scopus 로고
    • The UBA domain: A sequence motif present in multiple enzyme classes of the ubiquitination pathway
    • Hofmann, K. and Bucher, P. (1996) The UBA domain: a sequence motif present in multiple enzyme classes of the ubiquitination pathway. Trends Biochem. Sci., 21, 172-173.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 172-173
    • Hofmann, K.1    Bucher, P.2
  • 25
    • 0022967107 scopus 로고
    • Ubiquitin-lysozyme conjugates: Purification and susceptibility to proteolysis
    • Hough, R. and Rechsteiner, M. (1986) Ubiquitin-lysozyme conjugates: purification and susceptibility to proteolysis. J. Biol. Chem., 261, 2391-2399.
    • (1986) J. Biol. Chem. , vol.261 , pp. 2391-2399
    • Hough, R.1    Rechsteiner, M.2
  • 26
    • 0029561529 scopus 로고
    • Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene
    • Huang, Y., Baker, R.T. and Fischer-Vize, J.A. (1995) Control of cell fate by a deubiquitinating enzyme encoded by the fat facets gene. Science, 270, 1828-1831.
    • (1995) Science , vol.270 , pp. 1828-1831
    • Huang, Y.1    Baker, R.T.2    Fischer-Vize, J.A.3
  • 27
    • 0027053491 scopus 로고
    • The ubiquitin conjugation system
    • Jentsch, S. (1992) The ubiquitin conjugation system. Annu. Rev. Genet., 26, 177-205.
    • (1992) Annu. Rev. Genet. , vol.26 , pp. 177-205
    • Jentsch, S.1
  • 28
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson, E.S., Ma, P.C.M., Ota, I.M. and Varshavsky, A. (1995) A proteolytic pathway that recognizes ubiquitin as a degradation signal. J. Biol. Chem., 270, 17442-17456.
    • (1995) J. Biol. Chem. , vol.270 , pp. 17442-17456
    • Johnson, E.S.1    Ma, P.C.M.2    Ota, I.M.3    Varshavsky, A.4
  • 29
    • 0031038169 scopus 로고    scopus 로고
    • Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome
    • Lam, Y.A., Xu, W., DeMartino, G.N. and Cohen, R.E. (1997) Editing of ubiquitin conjugates by an isopeptidase in the 26S proteasome. Nature, 385, 737-740.
    • (1997) Nature , vol.385 , pp. 737-740
    • Lam, Y.A.1    Xu, W.2    DeMartino, G.N.3    Cohen, R.E.4
  • 30
    • 0021679940 scopus 로고
    • The yeast ubiquitin gene: Head-to-tail repeats encoding a polyubiquitin precursor protein
    • Özkaynak, E., Finley, D. and Varshavsky, A. (1984) The yeast ubiquitin gene: head-to-tail repeats encoding a polyubiquitin precursor protein. Nature, 312, 663-666.
    • (1984) Nature , vol.312 , pp. 663-666
    • Özkaynak, E.1    Finley, D.2    Varshavsky, A.3
  • 31
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • Papa, F. and Hochstrasser, M. (1993) The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene. Nature, 366, 313-319.
    • (1993) Nature , vol.366 , pp. 313-319
    • Papa, F.1    Hochstrasser, M.2
  • 32
    • 0023472472 scopus 로고
    • Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa
    • Schägger, H. and von Jagow, G. (1987) Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. Anal. Biochem., 166, 368-379.
    • (1987) Anal. Biochem. , vol.166 , pp. 368-379
    • Schägger, H.1    Von Jagow, G.2
  • 33
    • 0025164762 scopus 로고
    • Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins
    • Seufert, W. and Jentsch, S. (1990) Ubiquitin-conjugating enzymes UBC4 and UBC5 mediate selective degradation of short-lived and abnormal proteins. EMBO J., 9, 543-550.
    • (1990) EMBO J. , vol.9 , pp. 543-550
    • Seufert, W.1    Jentsch, S.2
  • 35
    • 0025889016 scopus 로고
    • Cloning and characterization of a 20-kDa ubiquitin carrier protein from wheat that catalyzes multiubiquitin chain formation in vitro
    • Van Nocker, S. and Vierstra, R.D. (1991) Cloning and characterization of a 20-kDa ubiquitin carrier protein from wheat that catalyzes multiubiquitin chain formation in vitro. Proc. Natl Acad. Sci. USA, 88, 10297-10301.
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 10297-10301
    • Van Nocker, S.1    Vierstra, R.D.2
  • 36
    • 0027428769 scopus 로고
    • Multiubiquitin chains linked through lysine 48 are abundant in vivo and are competent intermediates in the ubiquitin proteolytic pathway
    • Van Nocker, S. and Vierstra, R.D. (1993) Multiubiquitin chains linked through lysine 48 are abundant in vivo and are competent intermediates in the ubiquitin proteolytic pathway. J. Biol. Chem., 268, 24766-24773.
    • (1993) J. Biol. Chem. , vol.268 , pp. 24766-24773
    • Van Nocker, S.1    Vierstra, R.D.2
  • 37
    • 0026766091 scopus 로고
    • The N-end rule
    • Varshavsky, A. (1992) The N-end rule. Cell, 69, 725-735.
    • (1992) Cell , vol.69 , pp. 725-735
    • Varshavsky, A.1
  • 38
    • 0023275830 scopus 로고
    • A family of yeast expression vectors containing the phage f1 intergenic region
    • Vernet, T., Dignard, D. and Thomas, D.Y. (1987) A family of yeast expression vectors containing the phage f1 intergenic region. Gene, 52, 225-233.
    • (1987) Gene , vol.52 , pp. 225-233
    • Vernet, T.1    Dignard, D.2    Thomas, D.Y.3
  • 39
    • 0029095673 scopus 로고
    • Roles of ubiquitinylation in proteolysis and cellular regulation
    • Wilkinson, K.D. (1995) Roles of ubiquitinylation in proteolysis and cellular regulation. Annu. Rev. Nutr., 15, 161-189.
    • (1995) Annu. Rev. Nutr. , vol.15 , pp. 161-189
    • Wilkinson, K.D.1
  • 40
    • 0002657323 scopus 로고    scopus 로고
    • Deubiquitinating enzymes
    • Peters, J.M., Finley, D. and Harris, R. (eds), Plenum Press, New York, in press
    • Wilkinson, K.D. and Hochstrasser, M. (1997) Deubiquitinating enzymes. In Peters, J.M., Finley, D. and Harris, R. (eds), Ubiquitin and the Biology of the Cell. Plenum Press, New York, in press.
    • (1997) Ubiquitin and the Biology of the Cell
    • Wilkinson, K.D.1    Hochstrasser, M.2
  • 41
    • 0028823598 scopus 로고
    • Metabolism of the polyubiquitin degradation signal: Structure, mechanism, and role of isopeptidase T
    • Wilkinson, K.D., Tashayev, V.L., O'Connor, L.B., Larsen, C.N., Kasperek, E. and Pickart, C.M. (1995) Metabolism of the polyubiquitin degradation signal: structure, mechanism, and role of isopeptidase T. Biochemistry, 34, 14535-14546.
    • (1995) Biochemistry , vol.34 , pp. 14535-14546
    • Wilkinson, K.D.1    Tashayev, V.L.2    O'Connor, L.B.3    Larsen, C.N.4    Kasperek, E.5    Pickart, C.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.