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Volumn 17, Issue 10, 1998, Pages 2759-2766

Degradation signals for ubiquitin system proteolysis in Saccharomyces cerevisiae

Author keywords

Degradation signals; Proteolysis; UBC6; UBC7; Ubiquitin

Indexed keywords

BETA GALACTOSIDASE; GLOBULAR PROTEIN; HYBRID PROTEIN; MEMBRANE PROTEIN; PROTEASOME; UBIQUITIN;

EID: 0032525130     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.10.2759     Document Type: Article
Times cited : (186)

References (57)
  • 1
    • 0028280447 scopus 로고
    • Sequence features that correlate with MHC restriction
    • Altuvia,Y., Berzofsky,J.A., Rosenfeld.R. and Margalit.H. (1994) Sequence features that correlate with MHC restriction. Mol. Immunol., 31, 1-19.
    • (1994) Mol. Immunol. , vol.31 , pp. 1-19
    • Altuvia1    Berzofsky2    Rosenfeld3    Margalit4
  • 2
    • 0023003380 scopus 로고
    • In vivo half-life of a protein is a function of its amino-terminal residue
    • Bachmair,A., Finley.D. and Varshavsky.A. (1986) In vivo half-life of a protein is a function of its amino-terminal residue. Science, 234, 179-186.
    • (1986) Science , vol.234 , pp. 179-186
    • Bachmair1    Finley2    Varshavsky3
  • 3
    • 0025050840 scopus 로고
    • The recognition component of the N-end rule pathway
    • Bartel,B., Wiinning,!. and Varshavsky.A. (1990) The recognition component of the N-end rule pathway. EMBO J., 9, 3179-3189.
    • (1990) EMBO J. , vol.9 , pp. 3179-3189
    • Bartel1    Wiinning2    Varshavsky3
  • 4
    • 0029985369 scopus 로고    scopus 로고
    • Degradation of subunits of the Sec Ip complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway
    • Biederer,T., Volkwein,C. and Sommer,T. (1996) Degradation of subunits of the Sec Ip complex, an integral component of the ER membrane, by the ubiquitin-proteasome pathway. EMBO J., 15, 2069-2076.
    • (1996) EMBO J. , vol.15 , pp. 2069-2076
    • Biederer1    Volkwein2    Sommer3
  • 5
    • 0030666729 scopus 로고    scopus 로고
    • Role of Cuelp in ubiquilination and degradation at the ER surface
    • Biederer,T, Volkwein.C. and Sommer.T. (1997) Role of Cuelp in ubiquilination and degradation at the ER surface. Science, 278, 1806-1809
    • (1997) Science , vol.278 , pp. 1806-1809
    • Biederer1    Volkwein2    Sommer3
  • 6
    • 0025114865 scopus 로고
    • Colocalized Iransmembrane determinants for ER degradation and subunit assembly explain the imracellular fate of TCR chains
    • BonifacinoJ.S., Cosson.P. and Klausner.R.D. (1990) Colocalized Iransmembrane determinants for ER degradation and subunit assembly explain the imracellular fate of TCR chains. Cell, 63, 503-513.
    • (1990) Cell , vol.63 , pp. 503-513
    • Bonifacino, J.S.1
  • 7
    • 0025885341 scopus 로고
    • Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum
    • BonifacinoJ.S., Cosson.P., Shah.N. and Klausner.R.D. (1991) Role of potentially charged transmembrane residues in targeting proteins for retention and degradation within the endoplasmic reticulum. EMBO J., 10, 2783-2793.
    • (1991) EMBO J. , vol.10 , pp. 2783-2793
    • Bonifacino1
  • 8
    • 0027198563 scopus 로고
    • Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATa2 repressor
    • Chen,R, Johnson,?., Sommer.T. Jentsch.S. and Hochstrasser.M. (1993) Multiple ubiquitin-conjugating enzymes participate in the in vivo degradation of the yeast MATa2 repressor. Cell, 74, 357-369.
    • (1993) Cell , vol.74 , pp. 357-369
    • Chen1    Johnson2    Sommer3    Jentsch4    Hochstrasser5
  • 9
    • 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
    • CiechanoverA1
  • 10
    • 0030297537 scopus 로고    scopus 로고
    • A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response
    • CoxJ.S. and Walter,?. (1996) A novel mechanism for regulating activity of a transcription factor that controls the unfolded protein response. Cell, 87, 391-404.
    • (1996) Cell , vol.87 , pp. 391-404
    • Cox, J.S.1
  • 11
    • 0028213449 scopus 로고
    • Heat-inducible degron: A method for constructing temperature-sensitive mutants
    • Dohmen.R.J., Wu.P. and Varshavsky.A. (1994) Heat-inducible degron: a method for constructing temperature-sensitive mutants. Science, 263, 1273-1276.
    • (1994) Science , vol.263 , pp. 1273-1276
  • 12
    • 0023654338 scopus 로고
    • Chemical synthesis and expression of a cassette adapted ubiquitin gene
    • Ecker,D.J., Khan.M.I., Marsh.J., Butt,T.R. and Crooke.S.T. (1987) Chemical synthesis and expression of a cassette adapted ubiquitin gene. J. Biol. Chem., 262, 3524-3527.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3524-3527
    • Ecker1    Khan2    Marsh3    Butt4    Crooke5
  • 13
    • 0028151096 scopus 로고
    • SSS1 encodes a stabilizing component of the Secol subcomplex of the yeast protein translocation apparatus
    • EsnauIt.Y., Feldheim.D., BIondel.M.O., Scheckman.R. and Kepes.F. (1994) SSS1 encodes a stabilizing component of the Secol subcomplex of the yeast protein translocation apparatus. J. Biol. Chem., 269, 27478-27485.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27478-27485
    • EsnauIt, Y.1
  • 14
    • 0023666139 scopus 로고
    • The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation and other stress
    • Finley.D., Ozkaynak.E. and Varshavsky.A. (1987) The yeast polyubiquitin gene is essential for resistance to high temperatures, starvation and other stress. Cell, 48, 1035-1046.
    • (1987) Cell , vol.48 , pp. 1035-1046
    • FinleyD1    OzkaynakE2    VarshavskyA3
  • 15
    • 10244239321 scopus 로고    scopus 로고
    • Life with 6000 genes
    • Goffeau,A. et al. (1996) Life with 6000 genes. Science, 274, 546-567.
    • (1996) Science , vol.274 , pp. 546-567
    • Goffeau, A.E.A.1
  • 16
    • 0026454716 scopus 로고
    • Regulation by proteolysis: Energy-dependent proteases and their targets
    • Gottesman.S. and Maurizi.M.R. (1992) Regulation by proteolysis: energy-dependent proteases and their targets. Microbiol. Rev., 56, 592-621.
    • (1992) Microbiol. Rev. , vol.56 , pp. 592-621
    • Gottesman, S.1
  • 17
    • 0020645052 scopus 로고
    • Yeast promoters and LacZ fusions designed to study expression of cloned genes in yeast
    • Guarente.L. (1983) Yeast promoters and LacZ fusions designed to study expression of cloned genes in yeast. Methods Enzymol., 101, 181-191.
    • (1983) Methods Enzymol. , vol.101 , pp. 181-191
    • GuarenteL1
  • 18
    • 0027418063 scopus 로고
    • PRE2, highly homologous to the human major histocompatibility complex RINGIO gene, codes for a yeast proteasome subunit necessary for chymotryptic activity and degradation of ubiquitinated proteins
    • Heinemeyer.W., Gruhler.A., Mohrle.V., Mahe.Y. and Wolf.D.H. (1993) PRE2, highly homologous to the human major histocompatibility complex RINGIO gene, codes for a yeast proteasome subunit necessary for chymotryptic activity and degradation of ubiquitinated proteins. J. Biol. Chem., 268, 5115-5120.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5115-5120
    • Heinemeyer1
  • 19
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko.A. and Ciechanover,A. (1992) The ubiquitin system for protein degradation. Anna. Rev. Biochem., 61, 761-807.
    • (1992) Anna. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko1    Ciechanover2
  • 20
    • 0030054178 scopus 로고    scopus 로고
    • Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis
    • Hicke.L. and Reizman.H. (1996) Ubiquitination of a yeast plasma membrane receptor signals its ligand-stimulated endocytosis. Cell, 84, 277-287.
    • (1996) Cell , vol.84 , pp. 277-287
    • HickeL1    ReizmanH2
  • 21
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitinproteasome pathway
    • Hiller,M.M., Finger.A., Schweiger.M. and Wolf.D.H. (1996) ER degradation of a misfolded luminal protein by the cytosolic ubiquitinproteasome pathway. Science, 273, 1725-1728.
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller1    Finger2    Schweiger3    Wolf4
  • 22
    • 0029867623 scopus 로고    scopus 로고
    • Proteasomes: Destruction as a programme
    • Hilt.W. and Wolf.D.H. (1996) Proteasomes: destruction as a programme. Trends Biochem. Sci., 21, 96-102.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 96-102
    • Hil1    Wolf2
  • 24
    • 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
    • HochstrasserM1
  • 25
    • 0029870836 scopus 로고    scopus 로고
    • Protein degradation or regulation: Ub the judge
    • Hochstrasser.M. (1996a) Protein degradation or regulation: Ub the judge. Cell, 84, 813-815.
    • (1996) Cell , vol.84 , pp. 813-815
    • HochstrasserM1
  • 26
    • 0030457014 scopus 로고    scopus 로고
    • Ubiquitin-dependent protein degradation
    • Hochstrasser.M. (1996b) Ubiquitin-dependent protein degradation. Anna. Rev. Genet., 30, 405-439.
    • (1996) Anna. Rev. Genet. , vol.30 , pp. 405-439
    • HochstrasserM1
  • 27
    • 0025331090 scopus 로고
    • In vivo degradation of a transcriptional regulator: The yeast oc2 repressor
    • Hochstrasser.M. and Varshavsky.A. (1990) In vivo degradation of a transcriptional regulator: the yeast oc2 repressor. Cell, 61, 697-708.
    • (1990) Cell , vol.61 , pp. 697-708
    • HochstrasserM1    VarshavskyA2
  • 28
    • 0029162583 scopus 로고
    • Selective protein degradation: A journey's end within the proteasome
    • Jentsch.S. and Schlenker.S. (1995) Selective protein degradation: a journey's end within the proteasome. Cell, 82, 881-884.
    • (1995) Cell , vol.82 , pp. 881-884
    • JentschS1    SchlenkerS2
  • 29
    • 0029119522 scopus 로고
    • A proteolytic pathway that recognizes ubiquitin as a degradation signal
    • Johnson,E.S., Ma.P.C, 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
    • Johnson1    Ma2    Ota3    Varshavsky4
  • 30
    • 0027511214 scopus 로고
    • Resistance to cadmium mediated by ubiquitin-dependent proteolysis
    • Jungmann.J., Reins,H.-A., Schobert.C. and Jentsch.S. (1993) Resistance to cadmium mediated by ubiquitin-dependent proteolysis. Nature, 361, 369-371.
    • (1993) Nature , vol.361 , pp. 369-371
    • Jungmann1    Reins2    Schobert3    Jentsch4
  • 31
    • 0030024281 scopus 로고    scopus 로고
    • Role of a peptide tagging system in degradation of proteins synthesised from damaged messenger RNA
    • Keiler.K.C, Wal'ler.P.R. and Sauer.R.T. (1996) Role of a peptide tagging system in degradation of proteins synthesised from damaged messenger RNA. Science, 171, 990-993.
    • (1996) Science , vol.171 , pp. 990-993
    • Keiler, K.C.1
  • 32
    • 0029807944 scopus 로고    scopus 로고
    • How proteolysis drives the cell cycle
    • King,R.W, Deshaies.RJ., Peters.J.M. and Kirschner.M.W. (1996) How proteolysis drives the cell cycle. Science, 274, 1652-1659.
    • (1996) Science , vol.274 , pp. 1652-1659
    • King1    Deshaies2    Peters3    Kirschner4
  • 33
    • 0028607143 scopus 로고
    • Regulated degradation of the transcription factor Gcn4
    • Kornitzer.D., Raboy.B., Kulka.R.G. and Fink.G.R. (1994) Regulated degradation of the transcription factor Gcn4. EMBO J., 13, 6021-6030.
    • (1994) EMBO J. , vol.13 , pp. 6021-6030
    • Kornitzer, D.1
  • 34
    • 0020475449 scopus 로고
    • A simple method for displaying the hydropathic character of a protein
    • Kyte, J. and Doolittle.R.F. (1982) A simple method for displaying the hydropathic character of a protein. J. Mol. Biol., 157, 105-132.
    • (1982) J. Mol. Biol. , vol.157 , pp. 105-132
    • Kyte, J.1    Doolittle, R.F.2
  • 35
    • 0029075883 scopus 로고
    • Reversible phosphorylation controls the activity of cyclosome-associated cyclin-ubiquitin ligase
    • Lahav-Baratz.S., Sudakin.V., Ruderman,J.V. and Hershko.A. (1995) Reversible phosphorylation controls the activity of cyclosome-associated cyclin-ubiquitin ligase. Proc. Natl Acad. Sci. USA, 92, 9303-9307.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 9303-9307
    • Lahav-Baratz1    Sudakin2    Ruderman3    Hershko4
  • 36
    • 0029670193 scopus 로고    scopus 로고
    • Rapid degradation of the Gl cyclin CIn2 induced by CDK-dependent phosphorylation
    • Lanker.S., Valdivieso.M.H. and Wittenberg.C. (1996) Rapid degradation of the Gl cyclin CIn2 induced by CDK-dependent phosphorylation. Science, 271, 1597-1601.
    • (1996) Science , vol.271 , pp. 1597-1601
    • Lanker1
  • 37
    • 0027457742 scopus 로고
    • Transmembrane domain length affects charge-mediated retention and degradation of proteins within the endoplasmic reticulum
    • Lankford.S.R, Cosson.R, BonifacinoJ.S. and Klausner.R.D. (1993) Transmembrane domain length affects charge-mediated retention and degradation of proteins within the endoplasmic reticulum. J. Biol. Cliem., 268, 4814-4820.
    • (1993) J. Biol. Cliem. , vol.268 , pp. 4814-4820
    • Lankford, S.R.1
  • 38
    • 0027427249 scopus 로고
    • The yeast DOA4 gene encodes a deubiquitinating enzyme related to a product of the human tre-2 oncogene
    • Papa.F.R. 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.R.1
  • 39
    • 0023087430 scopus 로고
    • Effect of heat shock on protein degradation in mammalian cells: Involvement of the ubiquitin system
    • Parag.H.A., Raboy.B. and Kulka.R.G. (1987) Effect of heat shock on protein degradation in mammalian cells: involvement of the ubiquitin system. EMBO J., 6, 55-61.
    • (1987) EMBO J. , vol.6 , pp. 55-61
    • Parag, H.A.1
  • 40
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper.R.K., Bomler.S., BordalloJ., Sommer.T. and Wolf.D.H. (1997) Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature, 388, 891-895.
    • (1997) Nature , vol.388 , pp. 891-895
  • 42
    • 0030200110 scopus 로고    scopus 로고
    • PEST sequences and regulation by proteolysis
    • Rechsteiner, M. and Rogers.S.W. (1996) PEST sequences and regulation by proteolysis. Trends Biochem. Sci., 21, 267-271.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 267-271
    • Rechsteiner, M.1
  • 43
    • 0029353809 scopus 로고
    • The proteasome: A protein-degrading organelle? Curr
    • Rubin.D.M. and Finley.D. (1995) The proteasome: a protein-degrading organelle? Curr. Biol., 5, 854-858.
    • (1995) Biol. , vol.5 , pp. 854-858
    • Rubin, D.M.1
  • 44
    • 0020980522 scopus 로고
    • Easy identification of cDNA clones
    • Ruther.U. and Miiller-Hill.B. (1983) Easy identification of cDNA clones. EMBO J., 2, 1791-1794.
    • (1983) EMBO J. , vol.2 , pp. 1791-1794
    • RutherU1    Miiller-HillB2
  • 45
    • 0029002717 scopus 로고
    • Synthetic signals for ubiquitin-dependent proteolysis
    • Sadis.S., Atienza.C.Jr and Finley.D. (1995) Synthetic signals for ubiquitin-dependent proteolysis. Mol. Cell. Biol., 15, 4086-4094.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 4086-4094
    • Sadis, S.1
  • 47
    • 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
    • Seufert1    Jentsch2
  • 48
    • 0025632969 scopus 로고
    • VBC1 encodes a novel member of an essential subfamily of yeast ubiquitin-conjugating enzymes involved in protein degradation
    • Seufert,W., McGrathJ.P. and Jentsch.S. (1990) VBC1 encodes a novel member of an essential subfamily of yeast ubiquitin-conjugating enzymes involved in protein degradation. EMBO J., 9, 4535-4541.
    • (1990) EMBO J. , vol.9 , pp. 4535-4541
    • Seufert1    McGrath2
  • 49
    • 0028967267 scopus 로고
    • Role of a ubiquitin-conjugating enzyme in degradation of S- And M-phase cyclins
    • Seufert,W., Futcher.B. and Jentsch.S. (1995) Role of a ubiquitin-conjugating enzyme in degradation of S- and M-phase cyclins. Nature, 373, 78-81.
    • (1995) Nature , vol.373 , pp. 78-81
    • Seufert1    Futcher2    Jentsch3
  • 51
    • 0026090063 scopus 로고
    • In vitro mutagenesis and plasmid shuffling: From cloned gene to mutant yeast
    • Sikorski.R.S. and BoekeJ.D. (1991) In vitro mutagenesis and plasmid shuffling: from cloned gene to mutant yeast. Methods Enzymol., 194, 302-318.
    • (1991) Methods Enzymol. , vol.194 , pp. 302-318
    • Sikorski, R.S.1
  • 52
    • 0024669291 scopus 로고
    • A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae
    • Sikorski.R.S. and Hieter.P. (1989) A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics, 122, 19-27.
    • (1989) Genetics , vol.122 , pp. 19-27
  • 53
    • 0027327659 scopus 로고
    • A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum
    • Sommer.T. and Jentsch.S. (1993) A protein translocation defect linked to ubiquitin conjugation at the endoplasmic reticulum. Nature, 365, 176-179.
    • (1993) Nature , vol.365 , pp. 176-179
    • SommerT1    JentschS2
  • 54
    • 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
    • VarshavskyA1
  • 55
    • 0026782393 scopus 로고
    • The Pas2 protein essential for peroxisome biogenesis is related to ubiquitin-conjugating enzymes
    • Wiebel.F.F. and Kunau.W.H. (1992) The Pas2 protein essential for peroxisome biogenesis is related to ubiquitin-conjugating enzymes. Nature, 359, 73-76.
    • (1992) Nature , vol.359 , pp. 73-76
    • Wiebel, F.F.1
  • 56
    • 0029828991 scopus 로고    scopus 로고
    • Secol-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz,E.J., Tortorella,D., Bogyo,M., Yu,J., Mothes.W., Jones.T.R., Rapoport.T.A. and Ploegh.H.L. (1996) Secol-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature, 384, 432-438.
    • (1996) Nature , vol.384 , pp. 432-438
    • Wiert1    Tortorella2    Bogyo3    Yu4    Mothes5    Jones6    Rapoport7    Ploegh8
  • 57
    • 0028983369 scopus 로고
    • Cdc28-mediated control of Cln3 cyclin degradation
    • Cdc28-mediated control of Cln3 cyclin degradation. Mol. Cell. Biol., 15, 731-741.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 731-741
    • Yaglom1


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