메뉴 건너뛰기




Volumn 12, Issue 3, 1998, Pages 315-323

'ER degradation' of a mutant yeast plasma membrane protein by the ubiquitin-proteasome pathway

Author keywords

Proteasome; Ubiquitin; Uracil permease

Indexed keywords

PROTEASOME;

EID: 0031907211     PISSN: 08926638     EISSN: None     Source Type: Journal    
DOI: 10.1096/fasebj.12.3.315     Document Type: Article
Times cited : (25)

References (51)
  • 2
    • 0031128320 scopus 로고    scopus 로고
    • ER-associated and proteasome-mediated protein degradation: How two topologically restricted events came together
    • Brodsky, J. L., and McCracken, A. A. (1997) ER-associated and proteasome-mediated protein degradation: how two topologically restricted events came together. Trends Cell. Biol. 7, 151-154
    • (1997) Trends Cell. Biol. , vol.7 , pp. 151-154
    • Brodsky, J.L.1    McCracken, A.A.2
  • 3
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control, the cytoplasmic connection
    • Kopito, R. (1997) ER quality control, the cytoplasmic connection. Cell 88, 427-430
    • (1997) Cell , vol.88 , pp. 427-430
    • Kopito, R.1
  • 4
    • 0029985369 scopus 로고    scopus 로고
    • Degradation of subunits of the Sec61p 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 Sec61p 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
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 5
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M., Finger, A., Schweiger, M., and Wolf, D. H. (1996) ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway. Science 273, 1725-1728
    • (1996) Science , vol.273 , pp. 1725-1728
    • Hiller, M.1    Finger, A.2    Schweiger, M.3    Wolf, D.H.4
  • 6
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward, C. L., Omura, S., and Kopito, R. R. (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83, 121-127
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 7
    • 0030986960 scopus 로고    scopus 로고
    • Evidence of proteasome-mediated cytochrome P-450 degradation
    • Roberts, B. J. (1997) Evidence of proteasome-mediated cytochrome P-450 degradation. J. Biol. Chem. 272, 9771-9778
    • (1997) J. Biol. Chem. , vol.272 , pp. 9771-9778
    • Roberts, B.J.1
  • 8
    • 0030447659 scopus 로고    scopus 로고
    • Proteasome-dependent endoplasmic reticulum-associated protein degradation, an unconventional route to a familiar fate
    • Werner, E. D., Brodsky, J. L., and McCracken, A. A. (1996) Proteasome-dependent endoplasmic reticulum-associated protein degradation, an unconventional route to a familiar fate. Proc. Natl. Acad., Sci. USA 93, 13797-13801
    • (1996) Proc. Natl. Acad., Sci. USA , vol.93 , pp. 13797-13801
    • Werner, E.D.1    Brodsky, J.L.2    McCracken, A.A.3
  • 9
    • 0030789680 scopus 로고    scopus 로고
    • Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation
    • Pilon, M., Schekman, R., and Römisch, K. (1997) Sec61p mediates export of a misfolded secretory protein from the endoplasmic reticulum to the cytosol for degradation. EMBO J. 16, 4540-4568
    • (1997) EMBO J. , vol.16 , pp. 4540-4568
    • Pilon, M.1    Schekman, R.2    Römisch, K.3
  • 10
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper, R. K., Bör, S., Bordallo, J., Sommer, T., and Wolf, D. H. (1997) Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation. Nature (London) 388, 891-895
    • (1997) Nature (London) , vol.388 , pp. 891-895
    • Plemper, R.K.1    Bör, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 12
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methyglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein
    • Hampton, R. Y., Gardner, R. G., and Rine, J. (1996) Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methyglutaryl-CoA reductase, an integral endoplasmic reticulum membrane protein. Mol. Biol. Cell 7, 2029-2044
    • (1996) Mol. Biol. Cell , vol.7 , pp. 2029-2044
    • Hampton, R.Y.1    Gardner, R.G.2    Rine, J.3
  • 13
    • 0030041781 scopus 로고    scopus 로고
    • Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast
    • Knop, M., Finger, A., Braun, T., Hellmuth, K., and Wolf, D. H. (1996) Der1, a novel protein specifically required for endoplasmic reticulum degradation in yeast. EMBO J. 15, 753-763
    • (1996) EMBO J. , vol.15 , pp. 753-763
    • Knop, M.1    Finger, A.2    Braun, T.3    Hellmuth, K.4    Wolf, D.H.5
  • 14
    • 0026561138 scopus 로고
    • Intracellular trafficking defects in human disease
    • Amara, J. F., Cheng, S. H., and Smith, A. E. (1992) Intracellular trafficking defects in human disease. Trends Cell. Biol. 2, 145-149
    • (1992) Trends Cell. Biol. , vol.2 , pp. 145-149
    • Amara, J.F.1    Cheng, S.H.2    Smith, A.E.3
  • 16
    • 0027057980 scopus 로고
    • In vivo phosphorylation of the yeast uracil permease
    • Volland, C., Garnier, C., and Haguenauer-Tsapis, R. (1992) in vivo phosphorylation of the yeast uracil permease. J. Biol. Chem. 267, 23767-23771
    • (1992) J. Biol. Chem. , vol.267 , pp. 23767-23771
    • Volland, C.1    Garnier, C.2    Haguenauer-Tsapis, R.3
  • 17
    • 15844424064 scopus 로고    scopus 로고
    • Ubiquitination mediated by the Npil p/ Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease
    • Galan, J. M., Moreau, V., André, B., Volland, C., and Haguenauer-Tsapis, R. (1996) Ubiquitination mediated by the Npil p/ Rsp5p ubiquitin-protein ligase is required for endocytosis of the yeast uracil permease. J. Biol. Chem. 271, 10946-10952
    • (1996) J. Biol. Chem. , vol.271 , pp. 10946-10952
    • Galan, J.M.1    Moreau, V.2    André, B.3    Volland, C.4    Haguenauer-Tsapis, R.5
  • 18
    • 0030700220 scopus 로고    scopus 로고
    • Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins
    • in press
    • Hicke, L. (1997) Ubiquitin-dependent internalization and down-regulation of plasma membrane proteins. FASEB J. In press
    • (1997) FASEB J.
    • Hicke, L.1
  • 19
    • 0030881952 scopus 로고    scopus 로고
    • 63 is involved in ubiquitination of a yeast plasma membrane protein
    • 63 is involved in ubiquitination of a yeast plasma membrane protein. EMBO J. 16, 5847-5854
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.-M.1    Haguenauer-Tsapis, R.2
  • 20
    • 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
  • 22
    • 0026562884 scopus 로고
    • Improved method for high efficiency transformation of intact yeast cells
    • Gietz, D., St. Jean, A., Woods, R. A., and Schiestl, R. H. (1992) Improved method for high efficiency transformation of intact yeast cells. Nucleic Acid Res. 20, 1425
    • (1992) Nucleic Acid Res. , vol.20 , pp. 1425
    • Gietz, D.1    St Jean, A.2    Woods, R.A.3    Schiestl, R.H.4
  • 23
    • 0028307059 scopus 로고
    • Endocytosis and degradation of the yeast uracil permease under adverse conditions
    • Volland, C., Urban-Grimal, D., Géraud, G., and Haguenauer-Tsapis, R. (1994) Endocytosis and degradation of the yeast uracil permease under adverse conditions. J. Biol. Chem. 269, 9833-9841
    • (1994) J. Biol. Chem. , vol.269 , pp. 9833-9841
    • Volland, C.1    Urban-Grimal, D.2    Géraud, G.3    Haguenauer-Tsapis, R.4
  • 24
    • 0030990121 scopus 로고    scopus 로고
    • Physiological regulation of membrane sorting late in the secretory pathway of Saccharomyces cerevisiae
    • Roberg, K. J., Rowley, N., and Kaiser, C. A. (1997) Physiological regulation of membrane sorting late in the secretory pathway of Saccharomyces cerevisiae. J. Cell. Biol. 137, 1469-1482
    • (1997) J. Cell. Biol. , vol.137 , pp. 1469-1482
    • Roberg, K.J.1    Rowley, N.2    Kaiser, C.A.3
  • 25
    • 0027520458 scopus 로고
    • The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum
    • Esnault, Y., Blondel, M. O., Deshaies, R. J., Schekman, R., and Képès, F. (1993) The yeast SSS1 gene is essential for secretory protein translocation and encodes a conserved protein of the endoplasmic reticulum. EMBO J. 12, 4083-4093
    • (1993) EMBO J. , vol.12 , pp. 4083-4093
    • Esnault, Y.1    Blondel, M.O.2    Deshaies, R.J.3    Schekman, R.4    Képès, F.5
  • 29
    • 0030945486 scopus 로고    scopus 로고
    • Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast
    • Rayner, J. C., and Pelham, H. R. B. (1997) Transmembrane domain-dependent sorting of proteins to the ER and plasma membrane in yeast. EMBO J. 16, 1832-1841
    • (1997) EMBO J. , vol.16 , pp. 1832-1841
    • Rayner, J.C.1    Pelham, H.R.B.2
  • 30
    • 0025823035 scopus 로고
    • Compartimental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant
    • Graham, T. R., and Emr, S. (1991) Compartimental organization of Golgi-specific protein modification and vacuolar protein sorting events defined in a yeast sec18 (NSF) mutant. J. Cell Biol. 114, 207-218
    • (1991) J. Cell Biol. , vol.114 , pp. 207-218
    • Graham, T.R.1    Emr, S.2
  • 31
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K., and Goldberg, A. L. (1996) Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem. 65, 801-847
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 32
    • 0027418063 scopus 로고
    • PRE2, highly homologous to the human major histocompatibility complex-linked RING10 gene codes for a yeast proteasome subunit necessary for chymotryptic activity and degradation of ubiquitinated proteins
    • Heinemeyer, W., Gruhler, A., Möhrle, V., Mahé, Y., and Wolf, D. H. (1993) PRE2, highly homologous to the human major histocompatibility complex-linked RING10 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
    • Heinemeyer, W.1    Gruhler, A.2    Möhrle, V.3    Mahé, Y.4    Wolf, D.H.5
  • 33
    • 0028170682 scopus 로고
    • Degradation of the yeast MATα2 transcriptional regulator is mediated by the proteasome
    • Richter-Ruoff, B., Wolf, D. H., and Hochstrasser, M. (1994) Degradation of the yeast MATα2 transcriptional regulator is mediated by the proteasome. FEBS Lett. 354, 50-52
    • (1994) FEBS Lett. , vol.354 , pp. 50-52
    • Richter-Ruoff, B.1    Wolf, D.H.2    Hochstrasser, M.3
  • 34
    • 0027444947 scopus 로고
    • S. cerevisiae 26S protease mutants arrest division in G2/ metaphase
    • Ghislain, M. Udvardy, A., and Mann, C. (1993) S. cerevisiae 26S protease mutants arrest division in G2/ metaphase. Nature (London) 66, 358-362.
    • (1993) Nature (London) , vol.66 , pp. 358-362
    • Ghislain, M.1    Udvardy, A.2    Mann, C.3
  • 35
    • 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
  • 36
    • 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 (London) 365, 176-179
    • (1993) Nature (London) , vol.365 , pp. 176-179
    • Sommer, T.1    Jentsch, S.2
  • 37
    • 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
  • 38
    • 0030033982 scopus 로고    scopus 로고
    • Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome
    • van Nocker, S., Deveraux, Q., Rechsteiner, M., and Vierstra, R. D. (1996) Arabidopsis MBP1 gene encodes a conserved ubiquitin recognition component of the 26S proteasome. Proc. Natl. Acad. Sci. USA 93, 856-860
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 856-860
    • Van Nocker, S.1    Deveraux, Q.2    Rechsteiner, M.3    Vierstra, R.D.4
  • 39
    • 0029806477 scopus 로고    scopus 로고
    • The multiubiquitin-chain-binding Mcb1 is a component of 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover
    • van Nocker, S., Sadis, S., Rubin, D., Glickman, M., Fu, H., Coux, O., Wefes, I., Finley, D., and Vierstra, R. (1996) The multiubiquitin-chain-binding Mcb1 is a component of 26S proteasome in Saccharomyces cerevisiae and plays a nonessential, substrate-specific role in protein turnover. Mol. Cell. Biol. 16, 6020-6028
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 6020-6028
    • Van Nocker, S.1    Sadis, S.2    Rubin, D.3    Glickman, M.4    Fu, H.5    Coux, O.6    Wefes, I.7    Finley, D.8    Vierstra, R.9
  • 40
    • 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
  • 41
    • 0028815630 scopus 로고
    • Catabolite inactivation of fructose-1- 6-bisphosphatase of Saccharomyces cerevisiae
    • Schork, S. M., Thumm, M., and Wolf, D. H. (1995) Catabolite inactivation of fructose-1- 6-bisphosphatase of Saccharomyces cerevisiae. J. Biol. Chem. 270, 26446-26450
    • (1995) J. Biol. Chem. , vol.270 , pp. 26446-26450
    • Schork, S.M.1    Thumm, M.2    Wolf, D.H.3
  • 42
    • 0028146192 scopus 로고
    • Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant
    • Finley, D., Sadis, S., Monia, B. P., Boucher, P., Ecker, D. J., Crooke, S. T., and Chau, V. (1994) Inhibition of proteolysis and cell cycle progression in a multiubiquitination-deficient yeast mutant. Mol. Cell. Biol. 14, 5501-5509
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 5501-5509
    • Finley, D.1    Sadis, S.2    Monia, B.P.3    Boucher, P.4    Ecker, D.J.5    Crooke, S.T.6    Chau, V.7
  • 44
    • 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 (London) 366, 313-319
    • (1993) Nature (London) , vol.366 , pp. 313-319
    • Papa, F.R.1    Hochstrasser, M.2
  • 45
    • 0029163053 scopus 로고
    • Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus
    • Pelham, H. R. (1995) Sorting and retrieval between the endoplasmic reticulum and Golgi apparatus. Curr. Opin. Cell Biol. 7, 530-535
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 530-535
    • Pelham, H.R.1
  • 46
    • 0030812940 scopus 로고    scopus 로고
    • A di-acidic signal required for selective export from the endoplasmic reticulum
    • Nishimura, N., and Balch, W. E. (1997) A di-acidic signal required for selective export from the endoplasmic reticulum. Science 277, 556-558
    • (1997) Science , vol.277 , pp. 556-558
    • Nishimura, N.1    Balch, W.E.2
  • 47
    • 0029837381 scopus 로고    scopus 로고
    • Degradation of 3-hydroxy-3-methylglutaryl-CoAreductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis
    • McGee, T. P., Cheng, H., Kumagai, H., Omura, S., and Simoni, R. D. (1996) Degradation of 3-hydroxy-3-methylglutaryl-CoAreductase in endoplasmic reticulum membranes is accelerated as a result of increased susceptibility to proteolysis. J. Biol. Chem. 271, 25630-25638
    • (1996) J. Biol. Chem. , vol.271 , pp. 25630-25638
    • McGee, T.P.1    Cheng, H.2    Kumagai, H.3    Omura, S.4    Simoni, R.D.5
  • 48
    • 0028971506 scopus 로고
    • NPI1, an essential yeast gene involved in induced degradation of Gap 1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase
    • Hein, C., Springael, J. Y., Volland, C., Haguenauer-Tsapis, R., and André, B. (1995) NPI1, an essential yeast gene involved in induced degradation of Gap 1 and Fur4 permeases, encodes the Rsp5 ubiquitin-protein ligase. Mol. Microbiol. 18, 77-87
    • (1995) Mol. Microbiol. , vol.18 , pp. 77-87
    • Hein, C.1    Springael, J.Y.2    Volland, C.3    Haguenauer-Tsapis, R.4    André, B.5
  • 49
    • 0031961993 scopus 로고    scopus 로고
    • A PEST-like sequence mediates phosphorylation and efficient ubiquitination of the yeast uracil permease
    • In press
    • Marchal, C., Haguenauer-Tsapis, R., and Urban-Grimal, D. A PEST-like sequence mediates phosphorylation and efficient ubiquitination of the yeast uracil permease. Mol. Cell. Biol. In press
    • Mol. Cell. Biol.
    • Marchal, C.1    Haguenauer-Tsapis, R.2    Urban-Grimal, D.3
  • 50
    • 0028232167 scopus 로고
    • Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator
    • Pind, S., Riordan, J. R., and William, D. B. (1994) Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. (1994), 12784-12788
    • (1994) J. Biol. Chem. , vol.1994 , pp. 12784-12788
    • Pind, S.1    Riordan, J.R.2    William, D.B.3
  • 51
    • 0028881645 scopus 로고
    • Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituant of the ER quality control apparatus
    • Parlati, F., Dominguez, M., Bergeron, J. J. M., and Thomas, D. Y. (1995) Saccharomyces cerevisiae CNE1 encodes an endoplasmic reticulum (ER) membrane protein with sequence similarity to calnexin and calreticulin and functions as a constituant of the ER quality control apparatus. J. Biol. Chem. 270, 244-253
    • (1995) J. Biol. Chem. , vol.270 , pp. 244-253
    • Parlati, F.1    Dominguez, M.2    Bergeron, J.J.M.3    Thomas, D.Y.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.