메뉴 건너뛰기




Volumn 17, Issue 23, 1998, Pages 6879-6887

Perturbation of Hsp90 interaction with nascent CFTR prevents its maturation and accelerates its degradation by the proteasome

Author keywords

Ansamycin; CFTR; ER degradation; Hsp90; Proteasome

Indexed keywords

CALNEXIN; GELDANAMYCIN; HEAT SHOCK PROTEIN 70; HEAT SHOCK PROTEIN 90; HERBIMYCIN A; OLIGOSACCHARIDE; PROTEASOME; TRANSMEMBRANE CONDUCTANCE REGULATOR;

EID: 0032401771     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/17.23.6879     Document Type: Article
Times cited : (312)

References (57)
  • 1
    • 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
  • 2
    • 0030027968 scopus 로고    scopus 로고
    • Supervising the fold: Functional principles of molecular chaperones
    • Buchner, J. (1996) Supervising the fold: functional principles of molecular chaperones. FASEB J., 10, 10-19.
    • (1996) FASEB J. , vol.10 , pp. 10-19
    • Buchner, J.1
  • 3
    • 0027311276 scopus 로고
    • Protein kinase a (PKA) still activates CFTR chloride channel after mutagenesis of all ten PKa consensus phosphorylation sites
    • Chang, X.-B., Tabcharani, J.A., Hou, Y.-X., Jensen, T.J., Kartner, N., Alon, N., Hanrahan, J.W. and Riordan, J.R. (1993) Protein kinase A (PKA) still activates CFTR chloride channel after mutagenesis of all ten PKA consensus phosphorylation sites. J. Biol. Chem., 268, 11304-11311.
    • (1993) J. Biol. Chem. , vol.268 , pp. 11304-11311
    • Chang, X.-B.1    Tabcharani, J.A.2    Hou, Y.-X.3    Jensen, T.J.4    Kartner, N.5    Alon, N.6    Hanrahan, J.W.7    Riordan, J.R.8
  • 4
    • 0028241858 scopus 로고
    • Mapping of the cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion
    • Chang, X.-B., Hou, Y.-X., Jensen, T. and Riordan, J.R. (1994) Mapping of the cystic fibrosis transmembrane conductance regulator membrane topology by glycosylation site insertion. J. Biol. Chem., 269, 18572-18575.
    • (1994) J. Biol. Chem. , vol.269 , pp. 18572-18575
    • Chang, X.-B.1    Hou, Y.-X.2    Jensen, T.3    Riordan, J.R.4
  • 5
    • 0030689692 scopus 로고    scopus 로고
    • ATPase activity of purified multidrug resistance-associated protein
    • Chang, X.-B., Hou, Y.X. and Riordan, J.R. (1997) ATPase activity of purified multidrug resistance-associated protein. J. Biol. Chem., 272, 30962-30968.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30962-30968
    • Chang, X.-B.1    Hou, Y.X.2    Riordan, J.R.3
  • 6
    • 0029670034 scopus 로고    scopus 로고
    • p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2
    • Chavany, C. et al. (1996) p185erbB2 binds to GRP94 in vivo. Dissociation of the p185erbB2/GRP94 heterocomplex by benzoquinone ansamycins precedes depletion of p185erbB2. J. Biol. Chem., 271, 4974-4977.
    • (1996) J. Biol. Chem. , vol.271 , pp. 4974-4977
    • Chavany, C.1
  • 7
    • 0029049090 scopus 로고
    • Cotranslational folding and calnexin binding during glycoprotein synthesis
    • Chen, W., Helenius, J., Braakman, I. and Helenius, A. (1995) Cotranslational folding and calnexin binding during glycoprotein synthesis. Proc. Natl Acad. Sci. USA, 92, 6229-6233.
    • (1995) Proc. Natl Acad. Sci. USA , vol.92 , pp. 6229-6233
    • Chen, W.1    Helenius, J.2    Braakman, I.3    Helenius, A.4
  • 8
    • 0025987020 scopus 로고
    • Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel
    • Cheng, S.H., Rich, D.P., Marshall, J., Gregory, R.J., Welsh, M.J. and Smith, A.E. (1991) Phosphorylation of the R domain by cAMP-dependent protein kinase regulates the CFTR chloride channel. Cell, 66, 1027-1036.
    • (1991) Cell , vol.66 , pp. 1027-1036
    • Cheng, S.H.1    Rich, D.P.2    Marshall, J.3    Gregory, R.J.4    Welsh, M.J.5    Smith, A.E.6
  • 9
    • 0026523829 scopus 로고
    • Cystic fibrosis: Molecular biology and therapeutic implications
    • Collins, F.S. (1992) Cystic fibrosis: molecular biology and therapeutic implications. Science, 256, 774-779.
    • (1992) Science , vol.256 , pp. 774-779
    • Collins, F.S.1
  • 10
    • 0031586616 scopus 로고    scopus 로고
    • Geldanamycin prevents nuclear translocation of mutant p53
    • Dasgupta, G. and Momand, J. (1997) Geldanamycin prevents nuclear translocation of mutant p53. Exp. Cell Res., 237, 29-37.
    • (1997) Exp. Cell Res. , vol.237 , pp. 29-37
    • Dasgupta, G.1    Momand, J.2
  • 11
    • 0030989277 scopus 로고    scopus 로고
    • Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. the initial hsp90·p60·hsp70-dependent step is sufficient for creating the steroid binding conformation
    • Dittmar, K.D. and Pratt, W.B. (1997) Folding of the glucocorticoid receptor by the reconstituted Hsp90-based chaperone machinery. The initial hsp90·p60·hsp70-dependent step is sufficient for creating the steroid binding conformation. J. Biol. Chem., 272, 13047-13054.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13047-13054
    • Dittmar, K.D.1    Pratt, W.B.2
  • 12
    • 0029033981 scopus 로고
    • Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin
    • Fenteany, G., Standaert, R.F., Lane, W.S., Choi S., Corer, E.J. and Schreiber, S.L. (1995) Inhibition of proteasome activities and subunit-specific amino-terminal threonine modification by lactacystin. Science, 268, 726-731.
    • (1995) Science , vol.268 , pp. 726-731
    • Fenteany, G.1    Standaert, R.F.2    Lane, W.S.3    Choi, S.4    Corer, E.J.5    Schreiber, S.L.6
  • 13
    • 0028000734 scopus 로고
    • Immunochemical detection of the multidrug resistance-associated protein MRP in human multidrug-resistant tumor cells by monoclonal antibodies
    • Flens M.J., Izquierdo, M.A., Scheffer, G.L., Fritz, J.M., Meijer, C.J., Scheper, R.J. and Zaman, G.J. (1994) Immunochemical detection of the multidrug resistance-associated protein MRP in human multidrug-resistant tumor cells by monoclonal antibodies. Cancer Res., 54, 4557-4563.
    • (1994) Cancer Res. , vol.54 , pp. 4557-4563
    • Flens, M.J.1    Izquierdo, M.A.2    Scheffer, G.L.3    Fritz, J.M.4    Meijer, C.J.5    Scheper, R.J.6    Zaman, G.J.7
  • 14
    • 0031106603 scopus 로고    scopus 로고
    • Chaperones get in touch: The Hip-Hop connection
    • Frydman, J. and Hohfeld, J. (1997) Chaperones get in touch: the Hip-Hop connection. Trends Biochem. Sci., 22, 87-92.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 87-92
    • Frydman, J.1    Hohfeld, J.2
  • 15
    • 0030863995 scopus 로고    scopus 로고
    • The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation
    • Grenert, J.P. et al. (1997) The amino-terminal domain of heat shock protein 90 (hsp90) that binds geldanamycin is an ATP/ADP switch domain that regulates hsp90 conformation. J. Biol. Chem., 272, 23843-23850.
    • (1997) J. Biol. Chem. , vol.272 , pp. 23843-23850
    • Grenert, J.P.1
  • 16
    • 0028023828 scopus 로고
    • Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function
    • Hartson, S.D. and Matts, R.L. (1994) Association of Hsp90 with cellular Src-family kinases in a cell-free system correlates with altered kinase structure and function. Biochemistry, 33, 8912-8920.
    • (1994) Biochemistry , vol.33 , pp. 8912-8920
    • Hartson, S.D.1    Matts, R.L.2
  • 17
    • 0029024748 scopus 로고
    • Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum
    • Hebert, D.N., Foellmer, B. and Helenius, A. (1995) Glucose trimming and reglucosylation determine glycoprotein association with calnexin in the endoplasmic reticulum. Cell, 81, 425-433.
    • (1995) Cell , vol.81 , pp. 425-433
    • Hebert, D.N.1    Foellmer, B.2    Helenius, A.3
  • 18
    • 0028892084 scopus 로고
    • A role for Hsp90 in retinoid receptor signal transduction
    • Holley, S.J. and Yamamoto, K.R. (1995) A role for Hsp90 in retinoid receptor signal transduction. Mol. Biol. Cell, 6, 1833-1842.
    • (1995) Mol. Biol. Cell , vol.6 , pp. 1833-1842
    • Holley, S.J.1    Yamamoto, K.R.2
  • 19
    • 0028284571 scopus 로고
    • Assisting spontaneity: The role of Hsp90 and small Hsps as molecular chaperones
    • Jakob, U. and Buchner, J. (1994) Assisting spontaneity: the role of Hsp90 and small Hsps as molecular chaperones. Trends Biochem. Sci., 19, 25.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 25
    • Jakob, U.1    Buchner, J.2
  • 20
    • 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
  • 21
    • 0030809270 scopus 로고    scopus 로고
    • Protein folding in vivo: Unraveling complex pathways
    • Johnson, J.L. and Craig, E.A. (1997) Protein folding in vivo: unraveling complex pathways. Cell, 90, 201-204.
    • (1997) Cell , vol.90 , pp. 201-204
    • Johnson, J.L.1    Craig, E.A.2
  • 22
    • 0021852930 scopus 로고
    • Detection of P-glycoprotein in multidrug-resistant cell lines by monoclonal antibodies
    • Kartner, N., Evernden-Porelle, D., Bradley, G. and Ling, V. (1985) Detection of P-glycoprotein in multidrug-resistant cell lines by monoclonal antibodies. Nature, 316, 820-823.
    • (1985) Nature , vol.316 , pp. 820-823
    • Kartner, N.1    Evernden-Porelle, D.2    Bradley, G.3    Ling, V.4
  • 23
    • 0026073070 scopus 로고
    • Expression of the cystic fibrosis gene in non-epithelial invertebrate cells produces a regulated anion conductance
    • Kartner, N. et al. (1991) Expression of the cystic fibrosis gene in non-epithelial invertebrate cells produces a regulated anion conductance. Cell, 64, 681-691.
    • (1991) Cell , vol.64 , pp. 681-691
    • Kartner, N.1
  • 25
    • 0031891726 scopus 로고    scopus 로고
    • Geldanamycin, an hsp90/GRP94-binding drug, induces increased transcription of endoplasmic reticulum (ER) chaperones via the ER stress pathway
    • Lawson, B., Brewer, J.W. and Hendershot, L.M. (1998) Geldanamycin, an hsp90/GRP94-binding drug, induces increased transcription of endoplasmic reticulum (ER) chaperones via the ER stress pathway. J. Cell Physiol., 174, 170-178.
    • (1998) J. Cell Physiol. , vol.174 , pp. 170-178
    • Lawson, B.1    Brewer, J.W.2    Hendershot, L.M.3
  • 26
    • 0031021804 scopus 로고    scopus 로고
    • Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators
    • Loo, T.W. and Clarke, D.M. (1997) Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators. J. Biol. Chem., 272, 709-712.
    • (1997) J. Biol. Chem. , vol.272 , pp. 709-712
    • Loo, T.W.1    Clarke, D.M.2
  • 27
    • 0028559511 scopus 로고
    • Conformational maturation of CFTR but not its mutant counterpart (ΔF508) occurs in the endoplasmic reticulum and requires ATP
    • Lukacs, G.L., Mohamed, A., Kartner, N., Chang, X.-B., Riordan, J.R. and Grinstein, S. (1994) Conformational maturation of CFTR but not its mutant counterpart (ΔF508) occurs in the endoplasmic reticulum and requires ATP. EMBO J., 13, 6076-6086.
    • (1994) EMBO J. , vol.13 , pp. 6076-6086
    • Lukacs, G.L.1    Mohamed, A.2    Kartner, N.3    Chang, X.-B.4    Riordan, J.R.5    Grinstein, S.6
  • 28
    • 0029812759 scopus 로고    scopus 로고
    • Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin
    • Mimnaugh, E.G., Chavany, C. and Neckers, L. (1996) Polyubiquitination and proteasomal degradation of the p185c-erbB-2 receptor protein-tyrosine kinase induced by geldanamycin. J. Biol. Chem., 271, 22796-22801.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22796-22801
    • Mimnaugh, E.G.1    Chavany, C.2    Neckers, L.3
  • 29
    • 0031054643 scopus 로고    scopus 로고
    • Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins
    • Morris, J.A., Dorner, A.J., Edwards, C.A., Hendershot, L.M. and Kaufman, R.J. (1997) Immunoglobulin binding protein (BiP) function is required to protect cells from endoplasmic reticulum stress but is not required for the secretion of selective proteins. J. Biol. Chem., 272, 4327-4334.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4327-4334
    • Morris, J.A.1    Dorner, A.J.2    Edwards, C.A.3    Hendershot, L.M.4    Kaufman, R.J.5
  • 30
    • 0030324952 scopus 로고    scopus 로고
    • A pathway of multi-chaperone interactions common to diverse regulatory proteins: Estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1 and the aryl hydrocarbon receptor
    • Nair, S.C., Toran, E.J., Rimerman, R.A., Hjermstad, S., Smithgall, T.E. and Smith, D.F. (1996) A pathway of multi-chaperone interactions common to diverse regulatory proteins: estrogen receptor, Fes tyrosine kinase, heat shock transcription factor Hsf1 and the aryl hydrocarbon receptor. Cell Stress Chaperones, 1, 237-250.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 237-250
    • Nair, S.C.1    Toran, E.J.2    Rimerman, R.A.3    Hjermstad, S.4    Smithgall, T.E.5    Smith, D.F.6
  • 31
    • 0019485241 scopus 로고
    • A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein
    • Oppermann, H., Levinson, W. and Bishop, J.M. (1981) A cellular protein that associates with the transforming protein of Rous sarcoma virus is also a heat-shock protein. Proc. Natl Acad. Sci. USA, 78, 1067-1071.
    • (1981) Proc. Natl Acad. Sci. USA , vol.78 , pp. 1067-1071
    • Oppermann, H.1    Levinson, W.2    Bishop, J.M.3
  • 32
    • 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 Williams, 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., 269, 12784-12788.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12784-12788
    • Pind, S.1    Riordan, J.R.2    Williams, D.B.3
  • 33
    • 0030925683 scopus 로고    scopus 로고
    • Steroid receptor interactions with heat shock protein and immunophilin chaperones
    • Pratt, W.B. and Toft, D.O. (1997) Steroid receptor interactions with heat shock protein and immunophilin chaperones. Endocr. Rev., 18, 306-360.
    • (1997) Endocr. Rev. , vol.18 , pp. 306-360
    • Pratt, W.B.1    Toft, D.O.2
  • 34
    • 0031444238 scopus 로고    scopus 로고
    • Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone
    • Prodromou, C., Roe, S.M., O'Brien, R., Ladbury, J.E., Piper, P.W. and Pearl, L.H. (1997) Identification and structural characterization of the ATP/ADP-binding site in the Hsp90 molecular chaperone. Cell, 90, 65-75.
    • (1997) Cell , vol.90 , pp. 65-75
    • Prodromou, C.1    Roe, S.M.2    O'Brien, R.3    Ladbury, J.E.4    Piper, P.W.5    Pearl, L.H.6
  • 35
    • 0029997424 scopus 로고    scopus 로고
    • Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway
    • Qu, B.H. and Thomas, P.J. (1996) Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway. J. Biol. Chem., 271, 7261-7264.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7261-7264
    • Qu, B.H.1    Thomas, P.J.2
  • 36
    • 0029788023 scopus 로고    scopus 로고
    • Degradation of a mutant secretory protein, α1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity
    • Qu, D., Teckman, J.H., Omura, S. and Perlmutter, D.H. (1996) Degradation of a mutant secretory protein, α1-antitrypsin Z, in the endoplasmic reticulum requires proteasome activity. J. Biol. Chem., 271, 22791-22795.
    • (1996) J. Biol. Chem. , vol.271 , pp. 22791-22795
    • Qu, D.1    Teckman, J.H.2    Omura, S.3    Perlmutter, D.H.4
  • 37
    • 0031006695 scopus 로고    scopus 로고
    • Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding
    • Qu, B.H., Strickland, E.H. and Thomas, P.J. (1997) Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding. J. Biol. Chem., 272, 15739-15744.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15739-15744
    • Qu, B.H.1    Strickland, E.H.2    Thomas, P.J.3
  • 38
    • 0032539709 scopus 로고    scopus 로고
    • Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence
    • Scheibel, T., Weikl, T. and Buchner, J. (1998) Two chaperone sites in Hsp90 differing in substrate specificity and ATP dependence. Proc. Natl Acad. Sci. USA, 95, 1495-1499.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 1495-1499
    • Scheibel, T.1    Weikl, T.2    Buchner, J.3
  • 40
    • 0028906638 scopus 로고
    • cAMP-dependent protein kinase-mediated phosphorylation of cystic fibrosis transmembrane conductance regulator residue ser-753 and its role in channel activation
    • Seibert, F.S., Tabcharani, J.A., Chang, X.-B., Dulhanty, A.M., Mathews, C. Hanrahan, J.W. and Riordan, J.R. (1995) cAMP-dependent protein kinase-mediated phosphorylation of cystic fibrosis transmembrane conductance regulator residue ser-753 and its role in channel activation. J. Biol. Chem., 270, 2158-2162.
    • (1995) J. Biol. Chem. , vol.270 , pp. 2158-2162
    • Seibert, F.S.1    Tabcharani, J.A.2    Chang, X.-B.3    Dulhanty, A.M.4    Mathews, C.5    Hanrahan, J.W.6    Riordan, J.R.7
  • 41
    • 17544374096 scopus 로고    scopus 로고
    • Disease-associated mutations in the fourth cytoplasmic loop of CFTR compromise biosynthetic processing and chloride channel activity
    • Seibert, F.S., Linsdell, P., Loo, T.W., Hanrahan, J.W., Clarke, D.M. and Riordan, J.R. (1996) Disease-associated mutations in the fourth cytoplasmic loop of CFTR compromise biosynthetic processing and chloride channel activity. J. Biol. Chem., 271, 15139-15143.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15139-15143
    • Seibert, F.S.1    Linsdell, P.2    Loo, T.W.3    Hanrahan, J.W.4    Clarke, D.M.5    Riordan, J.R.6
  • 42
    • 15844363948 scopus 로고    scopus 로고
    • Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell
    • Sepehrnia, B., Paz, I.B., Dasgupta, G. and Momand, J. (1996) Heat shock protein 84 forms a complex with mutant p53 protein predominantly within a cytoplasmic compartment of the cell. J. Biol. Chem., 271, 15084-15090.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15084-15090
    • Sepehrnia, B.1    Paz, I.B.2    Dasgupta, G.3    Momand, J.4
  • 43
    • 0029684296 scopus 로고    scopus 로고
    • Involvement of molecular chaperones in intracellular protein breakdown
    • Sherman, M.Y. and Goldberg, A.L. (1996) Involvement of molecular chaperones in intracellular protein breakdown. Experientia Suppl., 77, 57-78.
    • (1996) Experientia Suppl. , vol.77 , pp. 57-78
    • Sherman, M.Y.1    Goldberg, A.L.2
  • 45
    • 0028828273 scopus 로고
    • Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent
    • Smith, D.F., Whitesell, L., Nair, S.C., Chen, S., Prapapanich, V. and Rimerman, R.A. (1995) Progesterone receptor structure and function altered by geldanamycin, an hsp90-binding agent. Mol. Cell. Biol., 15, 6804-6812.
    • (1995) Mol. Cell. Biol. , vol.15 , pp. 6804-6812
    • Smith, D.F.1    Whitesell, L.2    Nair, S.C.3    Chen, S.4    Prapapanich, V.5    Rimerman, R.A.6
  • 46
    • 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
    • Sommer, T.1    Jentsch, S.2
  • 47
    • 0030700576 scopus 로고    scopus 로고
    • Endoplasmic reticulum degradation: Reverse protein flow of no return
    • Sommer, T. and Wolf, D.H. (1997) Endoplasmic reticulum degradation: reverse protein flow of no return. FASEB J., 11, 1227-1233.
    • (1997) FASEB J. , vol.11 , pp. 1227-1233
    • Sommer, T.1    Wolf, D.H.2
  • 48
    • 0031005361 scopus 로고    scopus 로고
    • Crystal structure of an Hsp90-geldanamycin complex: Targeting of a protein chaperone by an antitumor agent
    • Stebbins, C.E., Russo, A.A., Schneider, C., Rosen, N., Hartl, F.U. and Pavletich, N.P. (1997) Crystal structure of an Hsp90-geldanamycin complex: targeting of a protein chaperone by an antitumor agent. Cell, 89, 239-250.
    • (1997) Cell , vol.89 , pp. 239-250
    • Stebbins, C.E.1    Russo, A.A.2    Schneider, C.3    Rosen, N.4    Hartl, F.U.5    Pavletich, N.P.6
  • 49
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the δ domain
    • Treier, M., Staszewski, L.M. and Bohmann, D. (1994) Ubiquitin-dependent c-Jun degradation in vivo is mediated by the δ domain. Cell, 787-798.
    • (1994) Cell , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 50
    • 0028352980 scopus 로고
    • Purification and characterization of an endogenous inhibitor specific to the Z-Leu-Leu-Leu-MCA degrading activity in proteasome and its identification as heat-shock protein 90
    • Tsubuki, S., Saito, Y. and Kawashima, S. (1994) Purification and characterization of an endogenous inhibitor specific to the Z-Leu-Leu-Leu-MCA degrading activity in proteasome and its identification as heat-shock protein 90. FEBS Lett, 344, 229-233.
    • (1994) FEBS Lett , vol.344 , pp. 229-233
    • Tsubuki, S.1    Saito, Y.2    Kawashima, S.3
  • 51
    • 0028889670 scopus 로고
    • Age-dependent association of isolated bovine lens multicatalytic proteinase complex (proteasome) with heat-shock protein 90, an endogenous inhibitor
    • Wagner, B.J. and Margolis, J.W. (1995) Age-dependent association of isolated bovine lens multicatalytic proteinase complex (proteasome) with heat-shock protein 90, an endogenous inhibitor. Arch. Biochem. Biophys., 323, 455-462.
    • (1995) Arch. Biochem. Biophys. , vol.323 , pp. 455-462
    • Wagner, B.J.1    Margolis, J.W.2
  • 52
    • 0028006681 scopus 로고
    • Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins
    • Ward, C.L. and Kopito, R.R. (1994) Intracellular turnover of cystic fibrosis transmembrane conductance regulator. Inefficient processing and rapid degradation of wild-type and mutant proteins. J. Biol. Chem., 269, 25710-25718.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 53
    • 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
  • 54
    • 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
  • 55
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-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) 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.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
  • 56
    • 0025157272 scopus 로고
    • The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein
    • Wilhelmsson, A., Cuthill, S., Denis, M., Wikstrom, A.C., Gustafsson, J.A. and Poellinger, L. (1990) The specific DNA binding activity of the dioxin receptor is modulated by the 90 kd heat shock protein. EMBO J., 9, 69-76.
    • (1990) EMBO J. , vol.9 , pp. 69-76
    • Wilhelmsson, A.1    Cuthill, S.2    Denis, M.3    Wikstrom, A.C.4    Gustafsson, J.A.5    Poellinger, L.6
  • 57
    • 0027488993 scopus 로고
    • The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment
    • Yang, Y., Janich, S., Cohn, J.A. and Wilson, J.M. (1993) The common variant of cystic fibrosis transmembrane conductance regulator is recognized by hsp70 and degraded in a pre-Golgi nonlysosomal compartment. Proc. Natl Acad. Sci. USA, 90, 9480-9484.
    • (1993) Proc. Natl Acad. Sci. USA , vol.90 , pp. 9480-9484
    • Yang, Y.1    Janich, S.2    Cohn, J.A.3    Wilson, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.