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Volumn 112, Issue 23, 1999, Pages 4185-4191

Surfing the Sec61 channel: Bidirectional protein translocation across the ER membrane

Author keywords

ER; Quality control; Sec61; Translocation; Yeast

Indexed keywords

MEMBRANE PROTEIN; MUTANT PROTEIN; SIGNAL PEPTIDE;

EID: 0033490112     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Note
Times cited : (130)

References (67)
  • 1
    • 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
  • 2
    • 0030666729 scopus 로고    scopus 로고
    • Role of Cue1p in ubiquitination and degradation at the ER surface
    • Biederer, T., Volkwein, C. and Sommer, T. (1997). Role of Cue1p in ubiquitination and degradation at the ER surface. Science 278, 1806-1809.
    • (1997) Science , vol.278 , pp. 1806-1809
    • Biederer, T.1    Volkwein, C.2    Sommer, T.3
  • 3
    • 0031885043 scopus 로고    scopus 로고
    • Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins
    • Bordallo, J., Plemper, R. K., Finger, A. and Wolf, D. H. (1998) Der3p/Hrd1p is required for endoplasmic reticulum-associated degradation of misfolded lumenal and integral membrane proteins. Mol. Biol. Cell 9, 209-222.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 209-222
    • Bordallo, J.1    Plemper, R.K.2    Finger, A.3    Wolf, D.H.4
  • 4
    • 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, 151-156.
    • (1997) Trends Cell Biol. , vol.7 , pp. 151-156
    • Brodsky, J.L.1    McCracken, A.A.2
  • 5
    • 0033208984 scopus 로고    scopus 로고
    • ER protein quality control and proteasome-mediated protein degradation
    • in press
    • Brodsky, J. L. and McCracken, A. A. (1999). ER protein quality control and proteasome-mediated protein degradation. Semin. Cell Dev. Biol. (in press).
    • (1999) Semin. Cell Dev. Biol.
    • Brodsky, J.L.1    McCracken, A.A.2
  • 6
    • 0033525198 scopus 로고    scopus 로고
    • The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct
    • Brodsky, J. L., Werner, E. D., Dubas, M. E., Goeckeler, J. L., Kruse, K. B. and McCracken, A. A. (1999). The requirement for molecular chaperones during endoplasmic reticulum-associated protein degradation demonstrates that protein export and import are mechanistically distinct. J. Biol. Chem. 274, 3453-3460.
    • (1999) J. Biol. Chem. , vol.274 , pp. 3453-3460
    • Brodsky, J.L.1    Werner, E.D.2    Dubas, M.E.3    Goeckeler, J.L.4    Kruse, K.B.5    McCracken, A.A.6
  • 7
    • 0030930513 scopus 로고    scopus 로고
    • The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae
    • Corsi, A. K. and Schekman, R. (1997). The lumenal domain of Sec63p stimulates the ATPase activity of BiP and mediates BiP recruitment to the translocon in Saccharomyces cerevisiae. J. Cell Biol. 137, 1483-1493.
    • (1997) J. Cell Biol. , vol.137 , pp. 1483-1493
    • Corsi, A.K.1    Schekman, R.2
  • 9
    • 0025970051 scopus 로고
    • Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex
    • Deshaies, R. J., Sanders, S. L., Feldheim, D. A. and Schekman, R. (1991). Assembly of yeast Sec proteins involved in translocation into the endoplasmic reticulum into a membrane-bound multisubunit complex. Nature 349, 806-808.
    • (1991) Nature , vol.349 , pp. 806-808
    • Deshaies, R.J.1    Sanders, S.L.2    Feldheim, D.A.3    Schekman, R.4
  • 10
    • 0032540384 scopus 로고    scopus 로고
    • Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome
    • deVirgilio, M., Weninger, H. and Ivessa, N. E. (1998). Ubiquitination is required for the retro-translocation of a short-lived luminal endoplasmic reticulum glycoprotein to the cytosol for degradation by the proteasome. J. Biol. Chem. 273, 9734-9743.
    • (1998) J. Biol. Chem. , vol.273 , pp. 9734-9743
    • Virgilio, M.1    Weninger, H.2    Ivessa, N.E.3
  • 11
    • 0342995731 scopus 로고    scopus 로고
    • The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process
    • Do, H., Falcone, D., Lin, J., Andrews, D. W. and Johnson, A. E. (1996). The cotranslational integration of membrane proteins into the phospholipid bilayer is a multistep process. Cell 85, 369-378.
    • (1996) Cell , vol.85 , pp. 369-378
    • Do, H.1    Falcone, D.2    Lin, J.3    Andrews, D.W.4    Johnson, A.E.5
  • 12
    • 0032476655 scopus 로고    scopus 로고
    • Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast
    • Enenkel, C., Lehmann, A. and Kloelzel, P. M. (1998) Subcellular distribution of proteasomes implicates a major location of protein degradation in the nuclear envelope-ER network in yeast. EMBO J. 17, 6144-6154.
    • (1998) EMBO J. , vol.17 , pp. 6144-6154
    • Enenkel, C.1    Lehmann, A.2    Kloelzel, P.M.3
  • 13
    • 0028151096 scopus 로고
    • SSSI encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus
    • Esnault, Y., Feldheim, D., Blondel, M. O., Schekman, R. and Kepes, F. (1994). SSSI encodes a stabilizing component of the Sec61 subcomplex of the yeast protein translocation apparatus. J. Biol. Chem. 269, 27478-27485.
    • (1994) J. Biol. Chem. , vol.269 , pp. 27478-27485
    • Esnault, Y.1    Feldheim, D.2    Blondel, M.O.3    Schekman, R.4    Kepes, F.5
  • 14
    • 0028022701 scopus 로고
    • Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex
    • Feldheim, D. and Schekman, R. (1994). Sec72p contributes to the selective recognition of signal peptides by the secretory polypeptide translocation complex. J. Cell Biol. 126, 935-943.
    • (1994) J. Cell Biol. , vol.126 , pp. 935-943
    • Feldheim, D.1    Schekman, R.2
  • 15
    • 0029881380 scopus 로고    scopus 로고
    • A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae
    • Finke, K., Plath, K., Panzner, S., Prehn, S., Rapoport, T. A., Hartmann, E. and Sommer, T. (1996). A second trimeric complex containing homologs of the Sec61p complex functions in protein transport across the ER membrane of S. cerevisiae. EMBO J. 15, 1482-1494.
    • (1996) EMBO J. , vol.15 , pp. 1482-1494
    • Finke, K.1    Plath, K.2    Panzner, S.3    Prehn, S.4    Rapoport, T.A.5    Hartmann, E.6    Sommer, T.7
  • 16
    • 0033559231 scopus 로고    scopus 로고
    • Phosphorylation of components of the ER translocation site
    • Gruss, O. J., Feick, P., Frank, R. and Dobberstein, B. (1999). Phosphorylation of components of the ER translocation site. Eur. J. Biochem. 260, 785-793.
    • (1999) Eur. J. Biochem. , vol.260 , pp. 785-793
    • Gruss, O.J.1    Feick, P.2    Frank, R.3    Dobberstein, B.4
  • 17
    • 0032549767 scopus 로고    scopus 로고
    • BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation
    • Hamman, B. D., Hendershot, L. M. and A. E. Johnson (1998). BiP maintains the permeability barrier of the ER membrane by sealing the lumenal end of the translocon pore before and early in translocation. Cell 92, 747-758.
    • (1998) Cell , vol.92 , pp. 747-758
    • Hamman, B.D.1    Hendershot, L.M.2    Johnson, A.E.3
  • 18
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • Hammond C. and Helenius A. (1995). Quality control in the secretory pathway. Curr. Opin. Cell Biol. 7, 523-529.
    • (1995) Curr. Opin. Cell Biol. , vol.7 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 19
    • 0029811218 scopus 로고    scopus 로고
    • Role of 26S proteasome and HRD genes in the degradation of 3-hydroxy-3-methylglutaryl-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-methylglutaryl-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
  • 21
    • 0029838640 scopus 로고    scopus 로고
    • ER degradation of a misfolded luminal protein by the cytosolic ubiquitin-proteasome pathway
    • Hiller, M. M., Finger, A., Schweiger, M. and Wolf, D. (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.M.1    Finger, A.2    Schweiger, M.3    Wolf, D.4
  • 22
    • 0031977709 scopus 로고    scopus 로고
    • Dissection of the translocation and chaperoning functions of yeast BiP/Kar2p in vivo
    • Holkeri, H. Paunola, E. Jamsa, E. and Makarow, M. (1998). Dissection of the translocation and chaperoning functions of yeast BiP/Kar2p in vivo. J. Cell Sci. 111, 749-757.
    • (1998) J. Cell Sci. , vol.111 , pp. 749-757
    • Holkeri, H.1    Paunola, E.2    Jamsa, E.3    Makarow, M.4
  • 23
    • 0029953675 scopus 로고    scopus 로고
    • Competition between folding and glycosylation in the endoplasmic reticulum
    • Holst, B., Bruun, A. W., Kielland-Brandt, M. C. and Winther, J. R. (1996). Competition between folding and glycosylation in the endoplasmic reticulum. EMBO J. 15, 3538-3546.
    • (1996) EMBO J. , vol.15 , pp. 3538-3546
    • Holst, B.1    Bruun, A.W.2    Kielland-Brandt, M.C.3    Winther, J.R.4
  • 24
    • 0030744415 scopus 로고    scopus 로고
    • The alpha chain of the T cell antigen receptor is degraded in the cytosol
    • Huppa, J. B. and Ploegh, H. L. (1997). The alpha chain of the T cell antigen receptor is degraded in the cytosol. Immunity 7, 113-122.
    • (1997) Immunity , vol.7 , pp. 113-122
    • Huppa, J.B.1    Ploegh, H.L.2
  • 26
    • 0032494135 scopus 로고    scopus 로고
    • Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure
    • Jakob, C. A., Burda, P., Roth, J. and Aebi, M. (1998). Degradation of misfolded endoplasmic reticulum glycoproteins in Saccharomyces cerevisiae is determined by a specific oligosaccharide structure. J. Cell Biol. 142, 1223-1233.
    • (1998) J. Cell Biol. , vol.142 , pp. 1223-1233
    • Jakob, C.A.1    Burda, P.2    Roth, J.3    Aebi, M.4
  • 27
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen T. J., Loo M. A., Pind, S., Williams, D. B., Goldberg, A. L. and Riordan, J. R. (1995). Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83, 129-135.
    • (1995) Cell , vol.83 , pp. 129-135
    • Jensen, T.J.1    Loo, M.A.2    Pind, S.3    Williams, D.B.4    Goldberg, A.L.5    Riordan, J.R.6
  • 28
    • 0029096050 scopus 로고
    • A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane
    • Jungnickel, B. and Rapoport, T. A. (1995). A posttargeting signal sequence recognition event in the endoplasmic reticulum membrane. Cell 82, 261-270.
    • (1995) Cell , vol.82 , pp. 261-270
    • Jungnickel, B.1    Rapoport, T.A.2
  • 29
    • 0031781639 scopus 로고    scopus 로고
    • The beta subunit of the See61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation
    • Kalies, K. U., Rapoport, T. A. and Hartmann, E. (1998). The beta subunit of the See61 complex facilitates cotranslational protein transport and interacts with the signal peptidase during translocation. J. Cell Biol. 41, 887-894.
    • (1998) J. Cell Biol. , vol.41 , pp. 887-894
    • Kalies, K.U.1    Rapoport, T.A.2    Hartmann, E.3
  • 30
    • 0025041029 scopus 로고
    • Protein degradation in the endoplasmic reticulum
    • Klausner R. D. and Sitia R. (1990). Protein degradation in the endoplasmic reticulum. Cell 62, 611-614.
    • (1990) Cell , vol.62 , pp. 611-614
    • Klausner, R.D.1    Sitia, R.2
  • 31
    • 0030041781 scopus 로고    scopus 로고
    • Der1, a novel protein specilically required for endoplasmic reticulum degradation in yeast
    • Knop, M., Finger, A., Braun, T., Hellmuth, K. and Wolf, D. H. (1996a) Der1, a novel protein specilically 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
  • 32
    • 0029817714 scopus 로고    scopus 로고
    • N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast
    • Knop, M., Hauser, N. and Wolf, D. H. (1996b). N-Glycosylation affects endoplasmic reticulum degradation of a mutated derivative of carboxypeptidase yscY in yeast. Yeast 12, 1229-1238.
    • (1996) Yeast , vol.12 , pp. 1229-1238
    • Knop, M.1    Hauser, N.2    Wolf, D.H.3
  • 33
    • 0032584722 scopus 로고    scopus 로고
    • Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control
    • Kowalski, J. M., Parekh, R. N., Mao, J. and Wittrup, K. D. (1998). Protein folding stability can determine the efficiency of escape from endoplasmic reticulum quality control. J. Biol. Chem. 273, 19453-19458.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19453-19458
    • Kowalski, J.M.1    Parekh, R.N.2    Mao, J.3    Wittrup, K.D.4
  • 34
    • 0032401771 scopus 로고    scopus 로고
    • Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome
    • Loo, M. A., Jensen, T. J., Cui, L., Hou, Y., Chang, X. B. and Riordan, J. R. (1998). Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome. EMBO J. 17, 6879-6887.
    • (1998) EMBO J. , vol.17 , pp. 6879-6887
    • Loo, M.A.1    Jensen, T.J.2    Cui, L.3    Hou, Y.4    Chang, X.B.5    Riordan, J.R.6
  • 36
    • 0030970268 scopus 로고    scopus 로고
    • Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP
    • Lyman, S. K. and Schekman, P. (1997). Binding of secretory precursor polypeptides to a translocon subcomplex is regulated by BiP. Cell 88, 85-96.
    • (1997) Cell , vol.88 , pp. 85-96
    • Lyman, S.K.1    Schekman, P.2
  • 37
    • 0032488845 scopus 로고    scopus 로고
    • Protein translocalion: Tunnel vision
    • Matlack, K. E., Mothes, W. and Rapoport, T. A. (1998). Protein translocalion: tunnel vision. Cell 92, 381-390.
    • (1998) Cell , vol.92 , pp. 381-390
    • Matlack, K.E.1    Mothes, W.2    Rapoport, T.A.3
  • 38
    • 0033612302 scopus 로고    scopus 로고
    • BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane
    • Matlack, K. E., Misselwitz, B., Plath, K. and Rapoport, T. A. (1999) BiP acts as a molecular ratchet during posttranslational transport of prepro-alpha factor across the ER membrane. Cell 97, 553-564.
    • (1999) Cell , vol.97 , pp. 553-564
    • Matlack, K.E.1    Misselwitz, B.2    Plath, K.3    Rapoport, T.A.4
  • 39
    • 0032526433 scopus 로고    scopus 로고
    • Role of the proteasome in membrane extraction of a short-lived F.R-transmembrane protein
    • Mayer, T. U., Braun, T. and Jentsch, S. (1998). Role of the proteasome in membrane extraction of a short-lived F.R-transmembrane protein. EMBO J. 17, 3251-3257.
    • (1998) EMBO J. , vol.17 , pp. 3251-3257
    • Mayer, T.U.1    Braun, T.2    Jentsch, S.3
  • 40
    • 0030070704 scopus 로고    scopus 로고
    • Assembly of ER-associated degradation in vitro: Dependence on cytosol, calnexin and ATP
    • McCracken, A. A. and Brodsky, J. L. (1996). Assembly of ER-associated degradation in vitro: dependence on cytosol, calnexin and ATP. J. Cell Biol. 132, 291-298.
    • (1996) J. Cell Biol. , vol.132 , pp. 291-298
    • McCracken, A.A.1    Brodsky, J.L.2
  • 41
    • 0032555650 scopus 로고    scopus 로고
    • Degradation of HMG-CoA reductase in vitro. Cleavage in the membrane domain by a membrane-bound cysteine protease
    • Moriyama, T., Sather, S. K., McGee, T. P. and Simoni, R. D. (1998). Degradation of HMG-CoA reductase in vitro. Cleavage in the membrane domain by a membrane-bound cysteine protease. J. Biol. Chem. 273, 22037-22043.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22037-22043
    • Moriyama, T.1    Sather, S.K.2    McGee, T.P.3    Simoni, R.D.4
  • 42
    • 0028997459 scopus 로고
    • Posttranslational protein transport in yeast reconstituted with a puritied complex of Sec proteins and Kar2p
    • Panzner, S., Dreier, L., Hartmann, E., Kostka, S. and Rapoport, T. A. (1995). Posttranslational protein transport in yeast reconstituted with a puritied complex of Sec proteins and Kar2p. Cell 81, 561-570.
    • (1995) Cell , vol.81 , pp. 561-570
    • Panzner, S.1    Dreier, L.2    Hartmann, E.3    Kostka, S.4    Rapoport, T.A.5
  • 43
    • 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, 4540-4548.
    • (1997) EMBO J. , vol.16 , pp. 4540-4548
    • Pilon, M.1    Schekman, R.2    Römisch, K.3
  • 44
    • 0031770876 scopus 로고    scopus 로고
    • Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane
    • Pilon, M., Römisch, K., Quach, D. and Schekman, R. (1998). Sec61p serves multiple roles in secretory precursor binding and translocation into the endoplasmic reticulum membrane. Mol. Biol. Cell 9, 3455-3473.
    • (1998) Mol. Biol. Cell , vol.9 , pp. 3455-3473
    • Pilon, M.1    Römisch, K.2    Quach, D.3    Schekman, R.4
  • 45
    • 0032544614 scopus 로고    scopus 로고
    • Signal sequence recognition in posttranslational protein transport across the yeast ER membrane
    • Plath, K., Mothes, W., Wilkinson, B. M., Stirling, C. J. and Rapoport, T. A. (1998). Signal sequence recognition in posttranslational protein transport across the yeast ER membrane. Cell 94, 795-807.
    • (1998) Cell , vol.94 , pp. 795-807
    • Plath, K.1    Mothes, W.2    Wilkinson, B.M.3    Stirling, C.J.4    Rapoport, T.A.5
  • 46
    • 1842409617 scopus 로고    scopus 로고
    • Mutant analysis links the translocon and BiP to retrograde protein transport for ER degradation
    • Plemper, R. K., Bohmler, 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 388, 891-895.
    • (1997) Nature , vol.388 , pp. 891-895
    • Plemper, R.K.1    Bohmler, S.2    Bordallo, J.3    Sommer, T.4    Wolf, D.H.5
  • 47
    • 0032484024 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome
    • Plemper, R. K., Egner, R., Kuchler, K. and Wolf, D. H. (1998). Endoplasmic reticulum degradation of a mutated ATP-binding cassette transporter Pdr5 proceeds in a concerted action of Sec61 and the proteasome. J. Biol. Chem. 273, 32848-32856.
    • (1998) J. Biol. Chem. , vol.273 , pp. 32848-32856
    • Plemper, R.K.1    Egner, R.2    Kuchler, K.3    Wolf, D.H.4
  • 48
    • 0033031194 scopus 로고    scopus 로고
    • Reentering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species
    • Plemper, R. K., Deak, P. M., Otto, R. T. and Wolf, D. H. (1999a) Reentering the translocon from the lumenal side of the endoplasmic reticulum. Studies on mutated carboxypeptidase yscY species. FEBS Lett. 443, 241-245.
    • (1999) FEBS Lett. , vol.443 , pp. 241-245
    • Plemper, R.K.1    Deak, P.M.2    Otto, R.T.3    Wolf, D.H.4
  • 49
    • 0033492290 scopus 로고    scopus 로고
    • Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation
    • in press
    • Plemper, R. K., Bordallo, J., Deak, P. M., Taxis, C., Hitt, R. and Wolf, D. H. (1999b). Genetic interactions of Hrd3p and Der3p/Hrd1p with Sec61p suggest a retro-translocation complex mediating protein transport for ER degradation. J. Cell Science 112 (in press).
    • (1999) J. Cell Science , vol.112
    • Plemper, R.K.1    Bordallo, J.2    Deak, P.M.3    Taxis, C.4    Hitt, R.5    Wolf, D.H.6
  • 50
    • 0030716878 scopus 로고    scopus 로고
    • The ins and outs of protein translocation
    • Riezman, H. (1997). The ins and outs of protein translocation. Science 278, 1228-1229.
    • (1997) Science , vol.278 , pp. 1228-1229
    • Riezman, H.1
  • 51
    • 0030986960 scopus 로고    scopus 로고
    • Evidence of proteasome-mediuted cytochrome P-450 degradation
    • Roberts, B. J. (1997). Evidence of proteasome-mediuted cytochrome P-450 degradation. J. Biol. Chem. 272, 9771-9778.
    • (1997) J. Biol. Chem. , vol.272 , pp. 9771-9778
    • Roberts, B.J.1
  • 52
    • 0026589260 scopus 로고
    • Sec61p and BiP directly facilitate polypeptide translocation into the ER
    • Sanders, S. L., Whitfield, K. M., Vogel, J. P., Rose, M. D. and Schekman, R. (1992). Sec61p and BiP directly facilitate polypeptide translocation into the ER. Cell 69, 353-365.
    • (1992) Cell , vol.69 , pp. 353-365
    • Sanders, S.L.1    Whitfield, K.M.2    Vogel, J.P.3    Rose, M.D.4    Schekman, R.5
  • 53
    • 0032555648 scopus 로고    scopus 로고
    • Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity
    • Suzuki, T., Park, H., Kitajima, K. and Lennarz, W. J. (1998). Peptides glycosylated in the endoplasmic reticulum of yeast are subsequently deglycosylated by a soluble peptide: N-glycanase activity. J. Biol. Chem. 273, 21526-21530.
    • (1998) J. Biol. Chem. , vol.273 , pp. 21526-21530
    • Suzuki, T.1    Park, H.2    Kitajima, K.3    Lennarz, W.J.4
  • 54
    • 0031045007 scopus 로고    scopus 로고
    • Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum
    • Tatu, U. and Helenius, A. (1997). Interactions between newly synthesized glycoproteins, calnexin and a network of resident chaperones in the endoplasmic reticulum. J. Cell Biol. 136, 555-565.
    • (1997) J. Cell Biol. , vol.136 , pp. 555-565
    • Tatu, U.1    Helenius, A.2
  • 55
    • 0029937560 scopus 로고    scopus 로고
    • Yeast protein translocation complex: Isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61 beta subunit
    • Toikkanen, J., Gatti, E., Takei, K., Saloheimo, M., Olkkonen, V. M., Soderlund, H., De Camilli, P. and Keranen, S. (1996). Yeast protein translocation complex: isolation of two genes SEB1 and SEB2 encoding proteins homologous to the Sec61 beta subunit. Yeast 12, 425-438.
    • (1996) Yeast , vol.12 , pp. 425-438
    • Toikkanen, J.1    Gatti, E.2    Takei, K.3    Saloheimo, M.4    Olkkonen, V.M.5    Soderlund, H.6    De Camilli, P.7    Keranen, S.8
  • 56
    • 0032572582 scopus 로고    scopus 로고
    • Dislocation of type I membrane proteins from the ER to the cytosol is sensitive to changes in redox potential
    • Tortorella, D., Story, C. M., Huppa, J. B., Wiertz, E. J. H. J., Jones, T. R. and Ploegh, H. L. (1998). Dislocation of type I membrane proteins from the ER to the cytosol is sensitive to changes in redox potential. J. Cell Biol. 142, 365-376.
    • (1998) J. Cell Biol. , vol.142 , pp. 365-376
    • Tortorella, D.1    Story, C.M.2    Huppa, J.B.3    Wiertz, E.J.H.J.4    Jones, T.R.5    Ploegh, H.L.6
  • 57
    • 0026347810 scopus 로고
    • Russell bodies: A general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum
    • Valetti, C., Grossi, C. E., Milstein, C. and Sitia, R. (1991) Russell bodies: a general response of secretory cells to synthesis of a mutant immunoglobulin which can neither exit from, nor be degraded in, the endoplasmic reticulum. J. Cell Biol. 115, 983-994.
    • (1991) J. Cell Biol. , vol.115 , pp. 983-994
    • Valetti, C.1    Grossi, C.E.2    Milstein, C.3    Sitia, R.4
  • 58
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • Ward C. L., Omura, S., 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
  • 59
    • 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. Nat. Acad. Sci. USA 93, 13797-13801.
    • (1996) Proc. Nat. Acad. Sci. USA , vol.93 , pp. 13797-13801
    • Werner, E.D.1    Brodsky, J.L.2    McCracken, A.A.3
  • 60
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus USl 11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • Wiertz, E. J., Jones, T. R., Sun, L., Bogyo, M., Geuze, H. J. and Ploegh, H. L. (1996a). The human cytomegalovirus USl 11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84, 769-779.
    • (1996) Cell , vol.84 , pp. 769-779
    • Wiertz, E.J.1    Jones, T.R.2    Sun, L.3    Bogyo, M.4    Geuze, H.J.5    Ploegh, H.L.6
  • 61
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • Wiertz, E. J. H. J., Tortorella, D., Bogyo, M., Yu, J., Mothes, W., Jones, T. R., Rapoport, T. A. and Ploegh, H. L. (1996b). Sec61-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
    • Wiertz, E.J.H.J.1    Tortorella, D.2    Bogyo, M.3    Yu, J.4    Mothes, W.5    Jones, T.R.6    Rapoport, T.A.7    Ploegh, H.L.8
  • 62
    • 0029817931 scopus 로고    scopus 로고
    • Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex
    • Wilkinson, B. M., Critchley, A. J. and Stirling, C. J. (1996). Determination of the transmembrane topology of yeast Sec61p, an essential component of the endoplasmic reticulum translocation complex. J. Biol. Chem. 271, 25590-25597.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25590-25597
    • Wilkinson, B.M.1    Critchley, A.J.2    Stirling, C.J.3
  • 63
    • 0030812436 scopus 로고    scopus 로고
    • Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p
    • Wilkinson, B. M., Esnault, Y., Craven, R. A., Skiba, F., Fieschi, J., Kepes, F. and Stirling, C. J. (1997). Molecular architecture of the ER translocase probed by chemical crosslinking of Sss1p to complementary fragments of Sec61p. EMBO J. 15, 4549-4559.
    • (1997) EMBO J. , vol.15 , pp. 4549-4559
    • Wilkinson, B.M.1    Esnault, Y.2    Craven, R.A.3    Skiba, F.4    Fieschi, J.5    Kepes, F.6    Stirling, C.J.7
  • 64
    • 0033614038 scopus 로고    scopus 로고
    • Evidence that endoplasmic reticulum (ER)-associated degradation of cystic fibrosis transmembrane conductance regulator is linked to retrograde translocation from the ER membrane
    • Xiong, X., Chong, E. and Skach, W. R. (1999). Evidence that endoplasmic reticulum (ER)-associated degradation of cystic fibrosis transmembrane conductance regulator is linked to retrograde translocation from the ER membrane. J. Biol. Chem. 274, 2616-2624.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2616-2624
    • Xiong, X.1    Chong, E.2    Skach, W.R.3
  • 65
    • 0032536903 scopus 로고    scopus 로고
    • Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: Importance of oligosaccharide processing. Ubiquitination and proteasorne-dependent removal from ER membranes
    • Yang, M., Omura, S., Bonifacino, J. S. and Weissman, A. M. (1998). Novel aspects of degradation of T cell receptor subunits from the endoplasmic reticulum (ER) in T cells: importance of oligosaccharide processing. ubiquitination and proteasorne-dependent removal from ER membranes. J. Exp. Med. 187, 835-846.
    • (1998) J. Exp. Med. , vol.187 , pp. 835-846
    • Yang, M.1    Omura, S.2    Bonifacino, J.S.3    Weissman, A.M.4
  • 66
    • 0028788228 scopus 로고
    • In vivo assembly of the proteasomal complexes, implications for antigen processing
    • Yang, Y., Fruh, K., Ahn, K. and Peterson, P. A. (1995). In vivo assembly of the proteasomal complexes, implications for antigen processing. J. Biol. Chem. 270, 27687-27694.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27687-27694
    • Yang, Y.1    Fruh, K.2    Ahn, K.3    Peterson, P.A.4
  • 67
    • 0027257647 scopus 로고
    • Regulation of selective protein degradation in the endoplasmic reticulum by redox potential
    • Young, J., Kane, P. L., Exley, M. and Wileman, T. (1993). Regulation of selective protein degradation in the endoplasmic reticulum by redox potential. J. Biol. Chem. 268, 19810-19818.
    • (1993) J. Biol. Chem. , vol.268 , pp. 19810-19818
    • Young, J.1    Kane, P.L.2    Exley, M.3    Wileman, T.4


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