메뉴 건너뛰기




Volumn 290, Issue 42, 2015, Pages 25636-25645

Combination of correctors rescue AF508-CFTR by reducing its association with Hsp40 and Hsp27

Author keywords

[No Author keywords available]

Indexed keywords

BINS; CELL CULTURE; CELL MEMBRANES; CELLS; CYTOLOGY; DISEASE CONTROL; SAWING;

EID: 84945207194     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M115.671925     Document Type: Article
Times cited : (37)

References (34)
  • 2
    • 84945239352 scopus 로고
    • Correction
    • Correction (1989) Science 245, 1347
    • (1989) Science , vol.245 , pp. 1347
  • 3
    • 0025349031 scopus 로고
    • Cystic fibrosis: A disease in electrolyte transport
    • Quinton, P. M. (1990) Cystic fibrosis: a disease in electrolyte transport. FASEB J. 4, 2709-2717
    • (1990) FASEB J. , vol.4 , pp. 2709-2717
    • Quinton, P.M.1
  • 4
    • 0031718588 scopus 로고    scopus 로고
    • Clinical implications of cystic fibrosis transmembrane conductance regulator mutations
    • Mickle, J. E., and Cutting, G. R. (1998) Clinical implications of cystic fibrosis transmembrane conductance regulator mutations. Clin. Chest Med. 19, 443-458
    • (1998) Clin. Chest Med. , vol.19 , pp. 443-458
    • Mickle, J.E.1    Cutting, G.R.2
  • 5
    • 79957946294 scopus 로고    scopus 로고
    • Managing cystic fibrosis: Strategies that increase life expectancy and improve quality of life
    • Cohen-Cymberknoh, M., Shoseyov, D., and Kerem, E. (2011) Managing cystic fibrosis: strategies that increase life expectancy and improve quality of life. Am. J. Respir. Crit Care Med. 183, 1463-1471
    • (2011) Am. J. Respir. Crit Care Med. , vol.183 , pp. 1463-1471
    • Cohen-Cymberknoh, M.1    Shoseyov, D.2    Kerem, E.3
  • 7
    • 50649123290 scopus 로고    scopus 로고
    • CFTR function and prospects for therapy
    • Riordan, J. R. (2008) CFTR function and prospects for therapy. Annu. Rev. Biochem. 77, 701-726
    • (2008) Annu. Rev. Biochem. , vol.77 , pp. 701-726
    • Riordan, J.R.1
  • 8
    • 78651247822 scopus 로고    scopus 로고
    • Sensitivity of chloride efflux vs. Transepithelial measurements in mixed CF and normal airway epithelial cell populations
    • Illek, B., Lei, D., Fischer, H., and Gruenert, D. C. (2010) Sensitivity of chloride efflux vs. transepithelial measurements in mixed CF and normal airway epithelial cell populations. Cell Physiol. Biochem. 26, 983-990
    • (2010) Cell Physiol. Biochem. , vol.26 , pp. 983-990
    • Illek, B.1    Lei, D.2    Fischer, H.3    Gruenert, D.C.4
  • 9
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • Jensen, T. J., and Loo, M. A., Pind, S., Williams, D. B., and 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
  • 13
    • 52049094378 scopus 로고    scopus 로고
    • Cystic fibrosis transmembrane regulator missing the first four transmembrane segments increases wild type and AF508 processing
    • Cebotaru, L., Vij, N, Ciobanu, I., Wright, J., Flotte, T., and Guggino, W. B. (2008) Cystic fibrosis transmembrane regulator missing the first four transmembrane segments increases wild type and AF508 processing. J. Biol. Chem. 283, 21926-21933
    • (2008) J. Biol. Chem. , vol.283 , pp. 21926-21933
    • Cebotaru, L.1    Vij, N.2    Ciobanu, I.3    Wright, J.4    Flotte, T.5    Guggino, W.B.6
  • 14
    • 84876239115 scopus 로고    scopus 로고
    • Transcomplementation by a truncation mutant of CFTR enhances AF508 processing through a biomolecualr interaction
    • Cebotaru, L., Woodward, O., Cebotaru, V., and Guggino, W. B. (2013) Transcomplementation by a truncation mutant of CFTR enhances AF508 processing through a biomolecualr interaction. J. Biol. Chem. 288, 10505-10512
    • (2013) J. Biol. Chem. , vol.288 , pp. 10505-10512
    • Cebotaru, L.1    Woodward, O.2    Cebotaru, V.3    Guggino, W.B.4
  • 15
    • 84896913799 scopus 로고    scopus 로고
    • Correcting the cystic fibrosis disease mutant, A455E CFTR
    • Cebotaru, L., Rapino, D., Cebotaru, V., and Guggino, W. B. (2014) Correcting the cystic fibrosis disease mutant, A455E CFTR. PLoS One 9, e85183
    • (2014) PLoS One , vol.9
    • Cebotaru, L.1    Rapino, D.2    Cebotaru, V.3    Guggino, W.B.4
  • 16
    • 24644464284 scopus 로고    scopus 로고
    • Small-molecule correctors of defective AF508-CFTR cellular processing identified by high-throughput screening
    • Pedemonte, N, and Lukacs, G. L., Du, K., Caci, E., Zegarra-Moran, O., Galietta, L. J., and Verkman, A. S. (2005) Small-molecule correctors of defective AF508-CFTR cellular processing identified by high-throughput screening. J. Clin. Invest. 115, 2564-2571
    • (2005) J. Clin. Invest. , vol.115 , pp. 2564-2571
    • Pedemonte, N.1    Lukacs, G.L.2    Du, K.3    Caci, E.4    Zegarra-Moran, O.5    Galietta, L.J.6    Verkman, A.S.7
  • 18
    • 84883448606 scopus 로고    scopus 로고
    • Rescuing mutant CFTR: A multitask approach to a better outcome in treating cystic fibrosis
    • Amaral, M. D., and Farinha, C.M. (2013) Rescuing mutant CFTR: a multitask approach to a better outcome in treating cystic fibrosis. Curr. Pharm. Des 19, 3497-3508
    • (2013) Curr. Pharm. Des , vol.19 , pp. 3497-3508
    • Amaral, M.D.1    Farinha, C.M.2
  • 22
  • 25
    • 0027380236 scopus 로고
    • The AF508 mutation decreases the stability of cystic fibrosis transmembrane conductance regulator in the plasma membrane: Determination of functional half-lives on transfected cells
    • Lukacs, G. L., and Chang, X. B., Bear, C, Kartner, N, Mohamed, A., Riordan, J. R., and Grinstein, S. (1993) The AF508 mutation decreases the stability of cystic fibrosis transmembrane conductance regulator in the plasma membrane: determination of functional half-lives on transfected cells. J. Biol. Chem. 268, 21592-21598
    • (1993) J. Biol. Chem. , vol.268 , pp. 21592-21598
    • Lukacs, G.L.1    Chang, X.B.2    Bear, C.3    Kartner, N.4    Mohamed, A.5    Riordan, J.R.6    Grinstein, S.7
  • 26
    • 2942580461 scopus 로고    scopus 로고
    • CFTR and chaperones: Processing and degradation
    • Amaral, M. D. (2004) CFTR and chaperones: processing and degradation. J. Mol. Neurosci. 23, 41-48
    • (2004) J. Mol. Neurosci. , vol.23 , pp. 41-48
    • Amaral, M.D.1
  • 28
    • 33947134399 scopus 로고    scopus 로고
    • Small heat-shock proteins select AF508-CFTR for endoplasmic reticulum-associated degradation
    • Ahner, A., Nakatsukasa, K., Zhang, H, and Frizzell, R. A., and Brodsky, J. L. (2007) Small heat-shock proteins select AF508-CFTR for endoplasmic reticulum-associated degradation. Mol. Biol. Cell 18, 806-814
    • (2007) Mol. Biol. Cell , vol.18 , pp. 806-814
    • Ahner, A.1    Nakatsukasa, K.2    Zhang, H.3    Frizzell, R.A.4    Brodsky, J.L.5
  • 29
    • 84872286562 scopus 로고    scopus 로고
    • Small heat shock proteins target mutant cystic fibrosis transmembrane conductance regulator for degradation via a small ubiquitin-like modifier-dependent pathway
    • Ahner, A., Gong, X., Schmidt, B. Z., and Peters, K. W., Rabeh, W. M., Thibodeau, P. H., Lukacs, G. L., and Frizzell, R. A. (2013) Small heat shock proteins target mutant cystic fibrosis transmembrane conductance regulator for degradation via a small ubiquitin-like modifier-dependent pathway. Mol. Biol. Cell 24, 74-84
    • (2013) Mol. Biol. Cell , vol.24 , pp. 74-84
    • Ahner, A.1    Gong, X.2    Schmidt, B.Z.3    Peters, K.W.4    Rabeh, W.M.5    Thibodeau, P.H.6    Lukacs, G.L.7    Frizzell, R.A.8
  • 30
    • 0037106481 scopus 로고    scopus 로고
    • The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by hsp70
    • Farinha, C. M., Nogueira, P., Mendes, F., Penque, D., and Amaral, M. D. (2002) The human DnaJ homologue (Hdj)-1/heat-shock protein (Hsp) 40 co-chaperone is required for the in vivo stabilization of the cystic fibrosis transmembrane conductance regulator by Hsp70. Biochem. J. 366, 797-806
    • (2002) Biochem. J. , vol.366 , pp. 797-806
    • Farinha, C.M.1    Nogueira, P.2    Mendes, F.3    Penque, D.4    Amaral, M.D.5
  • 31
    • 0027133280 scopus 로고
    • Effect of deletion mutations on the function of CFTR chloride channels
    • Rich, D. P., and Gregory, R. J., Cheng, S. H., Smith, A. E., and Welsh, M. J. (1993) Effect of deletion mutations on the function of CFTR chloride channels. Receptors Channels 1, 221-232
    • (1993) Receptors Channels , vol.1 , pp. 221-232
    • Rich, D.P.1    Gregory, R.J.2    Cheng, S.H.3    Smith, A.E.4    Welsh, M.J.5
  • 32
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most of cystic fibrosis
    • Cheng, S. H., Gregory, R. J., Marshall, J., Paul, S., Souza, D. W., White, G. A., O'Riordan, C. R., and Smith, A. E. (1990) Defective intracellular transport and processing of CFTR is the molecular basis of most of cystic fibrosis. Cell 63, 827-834
    • (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
  • 33
  • 34
    • 79954414554 scopus 로고    scopus 로고
    • Modeling general proteostasis: Proteome balance in health and disease
    • Roth, D. M., and Balch, W. E. (2011) Modeling general proteostasis: proteome balance in health and disease. Curr. Opin. Cell Biol. 23, 126-134
    • (2011) Curr. Opin. Cell Biol. , vol.23 , pp. 126-134
    • Roth, D.M.1    Balch, W.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.