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Volumn 79, Issue 1 SUPPL. 1, 1999, Pages

Biosynthesis and degradation of CFTR

Author keywords

[No Author keywords available]

Indexed keywords

CALNEXIN; CHAPERONE; HEAT SHOCK PROTEIN 70; MUTANT PROTEIN; NUCLEOTIDE BINDING PROTEIN; PROTEASOME; PROTEIN PRECURSOR; TRANSMEMBRANE CONDUCTANCE REGULATOR; UBIQUITIN;

EID: 0032957204     PISSN: 00319333     EISSN: None     Source Type: Journal    
DOI: 10.1152/physrev.1999.79.1.S167     Document Type: Review
Times cited : (376)

References (41)
  • 1
    • 0030154620 scopus 로고    scopus 로고
    • Chemical chaperones correct the mutant phenotype of the ΔF508 cystic fibrosis transmembrane conductance regulator protein
    • BROWN, C. R., L. Q. HONG-BROWN, J. BIWERSI, A. S. VERKMAN, AND W. J. WELCH. Chemical chaperones correct the mutant phenotype of the ΔF508 cystic fibrosis transmembrane conductance regulator protein. Cell Stress Chaperones 1: 117-125, 1996.
    • (1996) Cell Stress Chaperones , vol.1 , pp. 117-125
    • Brown, C.R.1    Hong-Brown, L.Q.2    Biwersi, J.3    Verkman, A.S.4    Welch, W.J.5
  • 2
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • CHENG, S. H., R. J. GREGORY, J. MARSHALL, S. PAUL, D. W. SOUZA, G. A. WHITE, C. R. O'RIORDAN, AND A. E. SMITH. Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell 63: 827-834, 1990.
    • (1990) Cell , vol.63 , pp. 827-834
    • Cheng, S.H.1    Gregory, R.J.2    Marshall, J.3    Paul, S.4    Souza, D.W.5    White, G.A.6    O'Riordan, C.R.7    Smith, A.E.8
  • 3
    • 0029835571 scopus 로고    scopus 로고
    • Effect of cystic fibrosis-associated mutations in the fourth intracellular loop of cystic fibrosis transmembrane conductance regulator
    • COTTEN, J. F., L. S. OSTEDGAARD, M. R. CARSON, AND M. J. WELSH. Effect of cystic fibrosis-associated mutations in the fourth intracellular loop of cystic fibrosis transmembrane conductance regulator. J. Biol. Chem. 271: 21279-21284, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 21279-21284
    • Cotten, J.F.1    Ostedgaard, L.S.2    Carson, M.R.3    Welsh, M.J.4
  • 5
    • 0026781952 scopus 로고
    • Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive
    • DENNING, G. M., M. P. ANDERSON, J. F. AMARA, J. MARSHALL, A. E. SMITH, AND M. J. WELSH. Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature 358: 761-764, 1992.
    • (1992) Nature , vol.358 , pp. 761-764
    • Denning, G.M.1    Anderson, M.P.2    Amara, J.F.3    Marshall, J.4    Smith, A.E.5    Welsh, M.J.6
  • 7
    • 0029040991 scopus 로고
    • Role of the endoplasmic reticulum chaperone calnexin in subunit folding and assembly of nicotinic: Acetylcholine receptors
    • GELMAN, M. S., W. CHANG, D. Y. THOMAS, J. J. BERGERON, AND J. M. PRIVES. Role of the endoplasmic reticulum chaperone calnexin in subunit folding and assembly of nicotinic: acetylcholine receptors. J. Biol. Chem. 270: 15085-15092, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15085-15092
    • Gelman, M.S.1    Chang, W.2    Thomas, D.Y.3    Bergeron, J.J.4    Prives, J.M.5
  • 8
    • 0025912486 scopus 로고
    • Maturation and function of cystic fibrosis transmembrane conductance regulator variants bearing mutations in putative nucleotide-binding domains 1 and 2
    • GREGORY, R. J., D. P. RICH, S. H. CHENG, D. W. SOUZA, S. PAUL, P. MANAVALAN, M. P. ANDERSON, M. J. WELSH, AND A. E. SMITH. Maturation and function of cystic fibrosis transmembrane conductance regulator variants bearing mutations in putative nucleotide-binding domains 1 and 2. Mol. Cell. Biol. 11: 3886-3893, 1991.
    • (1991) Mol. Cell. Biol. , vol.11 , pp. 3886-3893
    • Gregory, R.J.1    Rich, D.P.2    Cheng, S.H.3    Souza, D.W.4    Paul, S.5    Manavalan, P.6    Anderson, M.P.7    Welsh, M.J.8    Smith, A.E.9
  • 9
    • 0029094253 scopus 로고
    • Quality control in the secretory pathway
    • HAMMOND, C., AND A. HELENIUS. Quality control in the secretory pathway. Curr. Opin. Cell Biol. 1: 523-529, 1995.
    • (1995) Curr. Opin. Cell Biol. , vol.1 , pp. 523-529
    • Hammond, C.1    Helenius, A.2
  • 10
    • 0029992278 scopus 로고    scopus 로고
    • Molecular chaperones in cellular protein folding
    • HARTL, F. U. Molecular chaperones in cellular protein folding. Nature 381: 571-579, 1996.
    • (1996) Nature , vol.381 , pp. 571-579
    • Hartl, F.U.1
  • 11
    • 0028198111 scopus 로고
    • How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum
    • HELENIUS, A. How N-linked oligosaccharides affect glycoprotein folding in the endoplasmic reticulum. Mol. Biol. Cell 5: 253-265, 1994.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 253-265
    • Helenius, A.1
  • 12
    • 0024960594 scopus 로고
    • Transport proteins. Export-import family expands
    • HIGGINS, C. Transport proteins. Export-import family expands. Nature 340: 342, 1989.
    • (1989) Nature , vol.340 , pp. 342
    • Higgins, C.1
  • 13
    • 0023991287 scopus 로고
    • A family of closely related ATP-binding subunits from prokaryotic and eukaryotic cells
    • HIGGINS, C. F., M. P. GALLAGHER, M. L. MIMMACK, AND S. R. PEARCE. A family of closely related ATP-binding subunits from prokaryotic and eukaryotic cells. Bioessays 8: 111-116, 1988.
    • (1988) Bioessays , vol.8 , pp. 111-116
    • Higgins, C.F.1    Gallagher, M.P.2    Mimmack, M.L.3    Pearce, S.R.4
  • 14
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • JENSEN, T. J., M. A. LOO, S. PIND, D. B. WILLIAMS, A. L. GOLDBERG, AND J. R. RIORDAN. Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83: 129-135, 1995.
    • (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
  • 17
    • 0030949874 scopus 로고    scopus 로고
    • ER quality control: The cytoplasmic connection
    • KOPITO, R. R. ER quality control: the cytoplasmic connection. Cell 88: 427-430, 1997.
    • (1997) Cell , vol.88 , pp. 427-430
    • Kopito, R.R.1
  • 18
    • 0031021804 scopus 로고    scopus 로고
    • Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators
    • LOO, T. W., AND D. M. CLARKE. Correction of defective protein kinesis of human P-glycoprotein mutants by substrates and modulators. J. Biol. Chem. 272: 709-712, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 709-712
    • Loo, T.W.1    Clarke, D.M.2
  • 19
    • 0028559511 scopus 로고
    • Conformational maturation of CFTR but not its mutant counterpart (ΔF508) occurs in the endoplasmic reticulum and requires ATP
    • LUKACS, G. L., A. MOHAMED, N. KARTNER, X.-B. CHANG, J. R. RIORDAN, AND S. GRINSTEIN. Conformational maturation of CFTR but not its mutant counterpart (ΔF508) occurs in the endoplasmic reticulum and requires ATP. EMBOJ. 13: 6076-6086, 1994.
    • (1994) EMBOJ. , 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
  • 22
    • 0020616951 scopus 로고
    • Assembly in vivo of mouse muscle acetylcholine receptor: Identification of an alpha subunit species that may be an assembly intermediate
    • MERLIE, J. P., AND J. LINDSTROM. Assembly in vivo of mouse muscle acetylcholine receptor: identification of an alpha subunit species that may be an assembly intermediate. Cell 34: 747-757, 1983.
    • (1983) Cell , vol.34 , pp. 747-757
    • Merlie, J.P.1    Lindstrom, J.2
  • 24
    • 0028232167 scopus 로고
    • Participation of the endoplasmic reticulum chaperone calnexin (p88, IP90) in the biogenesis of the cystic fibrosis transmembrane conductance regulator
    • PIND, S., J. R. RIORDAN, AND D. B. WILLIAMS. 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.
    • (1994) J. Biol. Chem. , vol.269 , pp. 12784-12788
    • Pind, S.1    Riordan, J.R.2    Williams, D.B.3
  • 25
    • 0031006695 scopus 로고    scopus 로고
    • Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding
    • QU, B.-R, E. H. STRICKLAND, AND P. J. THOMAS. Localization and suppression of a kinetic defect in cystic fibrosis transmembrane conductance regulator folding. J. Biol. Chem. 272: 15739-15744, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15739-15744
    • Qu, B.-R.1    Strickland, E.H.2    Thomas, P.J.3
  • 26
    • 0029997424 scopus 로고    scopus 로고
    • Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway
    • QU, B. H., AND P. J. THOMAS. Alteration of the cystic fibrosis transmembrane conductance regulator folding pathway. J. Biol. Chem. 271: 7261-7264, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 7261-7264
    • Qu, B.H.1    Thomas, P.J.2
  • 28
    • 0026651895 scopus 로고
    • Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells
    • RIVETT, A. J., A. PALMER, AND E. KNECHT. Electron microscopic localization of the multicatalytic proteinase complex in rat liver and in cultured cells. J. Histochem. Cytochem. 40: 1165-1172, 1992.
    • (1992) J. Histochem. Cytochem. , vol.40 , pp. 1165-1172
    • Rivett, A.J.1    Palmer, A.2    Knecht, E.3
  • 30
    • 0023665223 scopus 로고
    • Phosphorylation and assembly of nicotinic acetylcholine receptor subunits in cultured chick muscle cells
    • ROSS, A. F., M. RAPUANO, J. H. SCHMIDT, AND J. M. PRIVES. Phosphorylation and assembly of nicotinic acetylcholine receptor subunits in cultured chick muscle cells. J. Biol. Chem. 262: 14640-14647, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 14640-14647
    • Ross, A.F.1    Rapuano, M.2    Schmidt, J.H.3    Prives, J.M.4
  • 31
    • 0032571366 scopus 로고    scopus 로고
    • Cotranslational ubiquitination of cystic fibrosis transmembrane conductance regulator in vitro
    • SATO, S., C. L. WARD, AND R. R. KOPITO. Cotranslational ubiquitination of cystic fibrosis transmembrane conductance regulator in vitro. J. Biol. Chem. 273: 7189-7192, 1998.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7189-7192
    • Sato, S.1    Ward, C.L.2    Kopito, R.R.3
  • 32
    • 0030042386 scopus 로고    scopus 로고
    • Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation
    • SATO, S., C. L. WARD, M. E. KROUSE, J. J. WINE, AND R. R. KOPITO. Glycerol reverses the misfolding phenotype of the most common cystic fibrosis mutation. J. Biol. Chem. 271: 635-638, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 635-638
    • Sato, S.1    Ward, C.L.2    Krouse, M.E.3    Wine, J.J.4    Kopito, R.R.5
  • 33
    • 17544374096 scopus 로고    scopus 로고
    • Disease-associated mutations in the fourth cytoplasmic loop of cystic fibrosis transmembrane conductance regulator compromise biosynthetic processing and chloride channel activity
    • SEIBERT, F. S., P. LINSDELL, T. W. LOO, J. W. HANRAHAN, D. M. CLARKE, AND J. R. RIORDAN. Disease-associated mutations in the fourth cytoplasmic loop of cystic fibrosis transmembrane conductance regulator compromise biosynthetic processing and chloride channel activity. J. Biol. Chem. 271: 15139-15145, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 15139-15145
    • Seibert, F.S.1    Linsdell, P.2    Loo, T.W.3    Hanrahan, J.W.4    Clarke, D.M.5    Riordan, J.R.6
  • 34
    • 0029910820 scopus 로고    scopus 로고
    • Cytoplasmic loop three of cystic fibrosis transmembrane conductance regulator contributes to regulation of chloride channel activity
    • SEIBERT, F. S., P. LINSDELL, T. W. LOO, J. W. HANRAHAN, J. R. RIORDAN, AND D. M. CLARKE. Cytoplasmic loop three of cystic fibrosis transmembrane conductance regulator contributes to regulation of chloride channel activity. J. Biol Chem. 271: 27493-27499, 1996.
    • (1996) J. Biol Chem. , vol.271 , pp. 27493-27499
    • Seibert, F.S.1    Linsdell, P.2    Loo, T.W.3    Hanrahan, J.W.4    Riordan, J.R.5    Clarke, D.M.6
  • 35
    • 15844397666 scopus 로고    scopus 로고
    • Contribution of proline residues in the membrane-spanning domains of cystic fibrosis transmembrane conductance regulator to chloride channel function
    • SHEPPARD, D. N., S. M. TRAVIS, H. ISHIHARA, AND M. J. WELSH. Contribution of proline residues in the membrane-spanning domains of cystic fibrosis transmembrane conductance regulator to chloride channel function. J. Biol. Chem. 271: 14995-15001, 1996.
    • (1996) J. Biol. Chem. , vol.271 , pp. 14995-15001
    • Sheppard, D.N.1    Travis, S.M.2    Ishihara, H.3    Welsh, M.J.4
  • 36
    • 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 R. R. KOPITO. 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.
    • (1994) J. Biol. Chem. , vol.269 , pp. 25710-25718
    • Ward, C.L.1    Kopito, R.R.2
  • 37
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin proteasome pathway
    • WARD, C. L., S. OMURA, AND R. R. KOPITO. Degradation of CFTR by the ubiquitin proteasome pathway. Cell 83: 121-127, 1995.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 38
    • 0029915568 scopus 로고    scopus 로고
    • The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol
    • WIERTZ, E. J., T. R. JONES, L. SUN, M. BOGYO, H. J. GEUZE, AND H. L. PLOEGH. The human cytomegalovirus US11 gene product dislocates MHC class I heavy chains from the endoplasmic reticulum to the cytosol. Cell 84: 769-779, 1996.
    • (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
  • 39
    • 0029828991 scopus 로고    scopus 로고
    • Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction
    • WIERTZ, E. J., D. TORTORELLA, M. BOGYO, J. YU, W. MOTHES, T. R. JONES, T. A. RAPOPORT, AND H. L. PLOEGH. Sec61-mediated transfer of a membrane protein from the endoplasmic reticulum to the proteasome for destruction. Nature 384: 432-438, 1996.
    • (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
  • 40
    • 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., S. JANICH, J. A. COHN, AMD J. M. WILSON. 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.
    • (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
  • 41
    • 0030817978 scopus 로고    scopus 로고
    • Cytosolic degradation of T-cell receptor alpha chains by the proteasome
    • YU, H., G. KAUNG, S. KOBAYASHI, AND R. R. KOPITO. Cytosolic degradation of T-cell receptor alpha chains by the proteasome. J. Biol. Chem. 272: 20800-20804, 1997.
    • (1997) J. Biol. Chem. , vol.272 , pp. 20800-20804
    • Yu, H.1    Kaung, G.2    Kobayashi, S.3    Kopito, R.R.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.