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Volumn 741, Issue , 2011, Pages 219-232

Analysis of CFTR Folding and Degradation in Transiently Transfected Cells

Author keywords

degradation; F508del; folding; pulse chase; Western blot

Indexed keywords

SMALL INTERFERING RNA; TRANSMEMBRANE CONDUCTANCE REGULATOR; UBIQUITIN PROTEIN LIGASE;

EID: 80052338631     PISSN: 10643745     EISSN: 19406029     Source Type: Book Series    
DOI: 10.1007/978-1-61779-117-8_15     Document Type: Chapter
Times cited : (12)

References (13)
  • 1
  • 2
    • 11444266284 scopus 로고    scopus 로고
    • The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR
    • Du, K., Sharma, M., and Lukacs, G. L. (2005) The DeltaF508 cystic fibrosis mutation impairs domain-domain interactions and arrests post-translational folding of CFTR. Nat. Struct. Mol. Biol. 12, 17–25.
    • (2005) Nat. Struct. Mol. Biol. , vol.12 , pp. 17-25
    • Du, K.1    Sharma, M.2    Lukacs, G.L.3
  • 3
    • 42149120706 scopus 로고    scopus 로고
    • Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function
    • Serohijos, A. W., Hegedus, T., Aleksandrov, A. A., He, L., Cui, L., Dokholyan, N. V., et al. (2008) Phenylalanine-508 mediates a cytoplasmic-membrane domain contact in the CFTR 3D structure crucial to assembly and channel function. Proc. Natl. Acad. Sci. USA 105, 3256–3261.
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 3256-3261
    • Serohijos, A.W.1    Hegedus, T.2    Aleksandrov, A.A.3    He, L.4    Cui, L.5    Dokholyan, N.V.6
  • 4
    • 0033559258 scopus 로고    scopus 로고
    • The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis
    • Meacham, G. C., Lu, Z., King, S., Sorscher, E., Tousson, A., and Cyr, D. M. (1999) The Hdj-2/Hsc70 chaperone pair facilitates early steps in CFTR biogenesis. EMBO J. 18, 1492–1505.
    • (1999) EMBO J , vol.18 , pp. 1492-1505
    • Meacham, G.C.1    Lu, Z.2    King, S.3    Sorscher, E.4    Tousson, A.5    Cyr, D.M.6
  • 5
    • 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
  • 6
    • 58149279835 scopus 로고    scopus 로고
    • Assembly and mis-assembly of CFTR: Folding defects caused by deletion of F508 occur before and after the calnexin-dependent association of MSD1 and MSD2. Mol. Biol
    • Rosser, M. F., Grove, D. E., Chen, L., and Cyr, D. M. (2008) Assembly and mis-assembly of CFTR: Folding defects caused by deletion of F508 occur before and after the calnexin-dependent association of MSD1 and MSD2. Mol. Biol. Cell 19, 4570–4579.
    • (2008) Cell , vol.19 , pp. 4570-4579
    • Rosser, M.F.1    Grove, D.E.2    Chen, L.3    Cyr, D.M.4
  • 7
    • 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
  • 8
    • 33750842131 scopus 로고    scopus 로고
    • Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis
    • Wang, X., Venable, J., LaPointe, P., Hutt, D. M., Koulov, A. V., Coppinger, J., et al. (2006) Hsp90 cochaperone Aha1 downregulation rescues misfolding of CFTR in cystic fibrosis. Cell 127, 803–815.
    • (2006) Cell , vol.127 , pp. 803-815
    • Wang, X.1    Venable, J.2    Lapointe, P.3    Hutt, D.M.4    Koulov, A.V.5    Coppinger, J.6
  • 9
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • Meacham, G. C., Patterson, C., Zhang, W., Younger, J. M., and Cyr, D. M. (2001) The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat. Cell. Biol. 3, 100–105.
    • (2001) Nat. Cell. Biol. , vol.3 , pp. 100-105
    • Meacham, G.C.1    Patterson, C.2    Zhang, W.3    Younger, J.M.4    Cyr, D.M.5
  • 10
    • 33746675669 scopus 로고    scopus 로고
    • Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator
    • Younger, J. M., Chen, L., Ren, H. Y., Rosser, M. F., Turnbull, E. L., Fan, C. Y., et al. (2006) Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell 126, 571–582.
    • (2006) Cell , vol.126 , pp. 571-582
    • Younger, J.M.1    Chen, L.2    Ren, H.Y.3    Rosser, M.F.4    Turnbull, E.L.5    Fan, C.Y.6
  • 11
    • 0742323006 scopus 로고    scopus 로고
    • Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway
    • Dalal, S., Rosser, M. F., Cyr, D. M., and Hanson, P. I. (2004) Distinct roles for the AAA ATPases NSF and p97 in the secretory pathway. Mol. Biol. Cell 15, 637–648.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 637-648
    • Dalal, S.1    Rosser, M.F.2    Cyr, D.M.3    Hanson, P.I.4
  • 12
    • 44949249968 scopus 로고    scopus 로고
    • Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTR{Delta}F508
    • Morito, D., Hirao, K., Oda, Y., Hosokawa, N., Tokunaga, F., Cyr, D. M., et al. (2008) Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTR{Delta}F508. Mol. Biol. Cell 19, 1328– 1336.
    • (2008) Mol. Biol. Cell , vol.19 , pp. 1328-1336
    • Morito, D.1    Hirao, K.2    Oda, Y.3    Hosokawa, N.4    Tokunaga, F.5    Cyr, D.M.6
  • 13
    • 44649096231 scopus 로고    scopus 로고
    • BAP31 interacts with Sec61 translocons and promotes retrotranslocation of CFTRDeltaF508 via the derlin-1 complex
    • Wang, B., Heath-Engel, H., Zhang, D., Nguyen, N., Thomas, D. Y., Hanrahan, J. W., et al. (2008) BAP31 interacts with Sec61 translocons and promotes retrotranslocation of CFTRDeltaF508 via the derlin-1 complex. Cell 133, 1080–1092.
    • (2008) Cell , vol.133 , pp. 1080-1092
    • Wang, B.1    Heath-Engel, H.2    Zhang, D.3    Nguyen, N.4    Thomas, D.Y.5    Hanrahan, J.W.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.