메뉴 건너뛰기




Volumn 8, Issue 6, 2013, Pages

Ubiquitination and Degradation of CFTR by the E3 Ubiquitin Ligase MARCH2 through Its Association with Adaptor Proteins CAL and STX6

Author keywords

[No Author keywords available]

Indexed keywords

ADAPTOR PROTEIN; BAFILOMYCIN A1; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR; CYSTIC FIBROSIS TRANSMEMBRANE CONDUCTANCE REGULATOR ASSOCIATED LIGAND; MARCH2 PROTEIN; SMALL INTERFERING RNA; SYNTAXIN 6; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 84879260385     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0068001     Document Type: Article
Times cited : (45)

References (50)
  • 1
    • 0024423668 scopus 로고
    • Identification of the cystic fibrosis gene: genetic analysis
    • doi: 10.1126/science.2570460
    • Kerem B, Rommens JM, Buchanan JA, Markiewicz D, Cox TK, et al. (1989) Identification of the cystic fibrosis gene: genetic analysis. Science 245: 1073-1080. doi:10.1126/science.2570460. PubMed: 2570460.
    • (1989) Science , vol.245 , pp. 1073-1080
    • Kerem, B.1    Rommens, J.M.2    Buchanan, J.A.3    Markiewicz, D.4    Cox, T.K.5
  • 2
    • 0024424270 scopus 로고
    • Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA
    • doi: 10.1126/science.2475911
    • Riordan JR, Rommens JM, Kerem B, Alon N, Rozmahel R, et al. (1989) Identification of the cystic fibrosis gene: cloning and characterization of complementary DNA. Science 245: 1066-1073. doi:10.1126/science.2475911. PubMed: 2475911.
    • (1989) Science , vol.245 , pp. 1066-1073
    • Riordan, J.R.1    Rommens, J.M.2    Kerem, B.3    Alon, N.4    Rozmahel, R.5
  • 3
    • 0032934916 scopus 로고    scopus 로고
    • Role of CFTR in airway disease
    • 9922383
    • Pilewski JM, Frizzell RA, (1999) Role of CFTR in airway disease. Physiol Rev 79: S215-S255. PubMed: 9922383.
    • (1999) Physiol Rev , vol.79
    • Pilewski, J.M.1    Frizzell, R.A.2
  • 4
    • 77956238947 scopus 로고    scopus 로고
    • c-Cbl facilitates endocytosis and lysosomal degradation of cystic fibrosis transmembrane conductance regulator in human airway epithelial cells
    • doi: 10.1074/jbc.M110.139881
    • Ye S, Cihil K, Stolz DB, Pilewski JM, Stanton BA, et al. (2010) c-Cbl facilitates endocytosis and lysosomal degradation of cystic fibrosis transmembrane conductance regulator in human airway epithelial cells. J Biol Chem 285: 27008-27018. doi:10.1074/jbc.M110.139881. PubMed: 20525683.
    • (2010) J Biol Chem , vol.285 , pp. 27008-27018
    • Ye, S.1    Cihil, K.2    Stolz, D.B.3    Pilewski, J.M.4    Stanton, B.A.5
  • 5
    • 84555189167 scopus 로고    scopus 로고
    • Dab2 is a key regulator of endocytosis and post-endocytic trafficking of the cystic fibrosis transmembrane conductance regulator
    • doi: 10.1042/BJ20111566
    • Fu L, Rab A, Tang LP, Rowe SM, Bebok Z, et al. (2012) Dab2 is a key regulator of endocytosis and post-endocytic trafficking of the cystic fibrosis transmembrane conductance regulator. Biochem J 441: 633-643. doi:10.1042/BJ20111566. PubMed: 21995445.
    • (2012) Biochem J , vol.441 , pp. 633-643
    • Fu, L.1    Rab, A.2    Tang, L.P.3    Rowe, S.M.4    Bebok, Z.5
  • 6
    • 0035142877 scopus 로고    scopus 로고
    • The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation
    • doi: 10.1038/35070137
    • Meacham GC, Patterson C, Zhang W, Younger JM, Cyr DM, (2001) The Hsc70 co-chaperone CHIP targets immature CFTR for proteasomal degradation. Nat Cell Biol 3: 100-105. doi:10.1038/35070137. PubMed: 11146634.
    • (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
  • 7
    • 33746675669 scopus 로고    scopus 로고
    • Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator
    • doi: 10.1016/j.cell.2006.06.041
    • Younger JM, Chen L, Ren HY, Rosser MF, Turnbull EL, et al. (2006) Sequential quality-control checkpoints triage misfolded cystic fibrosis transmembrane conductance regulator. Cell 126: 571-582. doi:10.1016/j.cell.2006.06.041. PubMed: 16901789.
    • (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
  • 8
    • 80051689133 scopus 로고    scopus 로고
    • Role of Hsc70 binding cycle in CFTR folding and endoplasmic reticulum-associated degradation
    • doi: 10.1091/mbc.E11-02-0137
    • Matsumura Y, David LL, Skach WR, (2011) Role of Hsc70 binding cycle in CFTR folding and endoplasmic reticulum-associated degradation. Mol Biol Cell 22: 2797-2809. doi:10.1091/mbc.E11-02-0137. PubMed: 21697503.
    • (2011) Mol Biol Cell , vol.22 , pp. 2797-2809
    • Matsumura, Y.1    David, L.L.2    Skach, W.R.3
  • 9
    • 67650520176 scopus 로고    scopus 로고
    • The deubiquitinating enzyme USP10 regulates the post-endocytic sorting of cystic fibrosis transmembrane conductance regulator in airway epithelial cells
    • doi: 10.1074/jbc.M109.001685
    • Bomberger JM, Barnaby RL, Stanton BA, (2009) The deubiquitinating enzyme USP10 regulates the post-endocytic sorting of cystic fibrosis transmembrane conductance regulator in airway epithelial cells. J Biol Chem 284: 18778-18789. doi:10.1074/jbc.M109.001685. PubMed: 19398555.
    • (2009) J Biol Chem , vol.284 , pp. 18778-18789
    • Bomberger, J.M.1    Barnaby, R.L.2    Stanton, B.A.3
  • 10
    • 63249095885 scopus 로고    scopus 로고
    • Cysteine string protein promotes proteasomal degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) by increasing its interaction with the C terminus of Hsp70-interacting protein and promoting CFTR ubiquitylation
    • 19098309
    • Schmidt BZ, Watts RJ, Aridor M, Frizzell RA, (2009) Cysteine string protein promotes proteasomal degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) by increasing its interaction with the C terminus of Hsp70-interacting protein and promoting CFTR ubiquitylation. J Biol Chem 284: 4168-4178. PubMed: 19098309.
    • (2009) J Biol Chem , vol.284 , pp. 4168-4178
    • Schmidt, B.Z.1    Watts, R.J.2    Aridor, M.3    Frizzell, R.A.4
  • 11
    • 33846008398 scopus 로고    scopus 로고
    • Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants
    • doi: 10.1074/jbc.M607085200
    • Sun F, Zhang R, Gong X, Geng X, Drain PF, et al. (2006) Derlin-1 promotes the efficient degradation of the cystic fibrosis transmembrane conductance regulator (CFTR) and CFTR folding mutants. J Biol Chem 281: 36856-36863. doi:10.1074/jbc.M607085200. PubMed: 16954204.
    • (2006) J Biol Chem , vol.281 , pp. 36856-36863
    • Sun, F.1    Zhang, R.2    Gong, X.3    Geng, X.4    Drain, P.F.5
  • 12
    • 77955607650 scopus 로고    scopus 로고
    • Peripheral protein quality control removes unfolded CFTR from the plasma membrane
    • doi: 10.1126/science.1191542
    • Okiyoneda T, Barrière H, Bagdány M, Rabeh WM, Du K, et al. (2010) Peripheral protein quality control removes unfolded CFTR from the plasma membrane. Science 329: 805-810. doi:10.1126/science.1191542. PubMed: 20595578.
    • (2010) Science , vol.329 , pp. 805-810
    • Okiyoneda, T.1    Barrière, H.2    Bagdány, M.3    Rabeh, W.M.4    Du, K.5
  • 13
    • 0028858161 scopus 로고
    • Multiple proteolytic systems, including the proteasome, contribute to CFTR processing
    • doi: 10.1016/0092-8674(95)90241-4
    • Jensen TJ, Loo MA, Pind S, Williams DB, Goldberg AL, et al. (1995) Multiple proteolytic systems, including the proteasome, contribute to CFTR processing. Cell 83: 129-135. doi:10.1016/0092-8674(95)90241-4. PubMed: 7553864.
    • (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
  • 14
    • 0028840915 scopus 로고
    • Degradation of CFTR by the ubiquitin-proteasome pathway
    • doi: 10.1016/0092-8674(95)90240-6
    • Ward CL, Omura S, Kopito RR, (1995) Degradation of CFTR by the ubiquitin-proteasome pathway. Cell 83: 121-127. doi:10.1016/0092-8674(95)90240-6. PubMed: 7553863.
    • (1995) Cell , vol.83 , pp. 121-127
    • Ward, C.L.1    Omura, S.2    Kopito, R.R.3
  • 15
    • 12144287602 scopus 로고    scopus 로고
    • Misfolding diverts CFTR from recycling to degradation: quality control at early endosomes
    • doi: 10.1083/jcb.200312018
    • Sharma M, Pampinella F, Nemes C, Benharouga M, So J, et al. (2004) Misfolding diverts CFTR from recycling to degradation: quality control at early endosomes. J Cell Biol 164: 923-933. doi:10.1083/jcb.200312018. PubMed: 15007060.
    • (2004) J Cell Biol , vol.164 , pp. 923-933
    • Sharma, M.1    Pampinella, F.2    Nemes, C.3    Benharouga, M.4    So, J.5
  • 16
    • 44949249968 scopus 로고    scopus 로고
    • Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508
    • doi: 10.1091/mbc.E07-06-0601
    • Morito D, Hirao K, Oda Y, Hosokawa N, Tokunaga F, et al. (2008) Gp78 cooperates with RMA1 in endoplasmic reticulum-associated degradation of CFTRDeltaF508. Mol Biol Cell 19: 1328-1336. doi:10.1091/mbc.E07-06-0601. PubMed: 18216283.
    • (2008) Mol Biol Cell , vol.19 , pp. 1328-1336
    • Morito, D.1    Hirao, K.2    Oda, Y.3    Hosokawa, N.4    Tokunaga, F.5
  • 17
    • 70549109093 scopus 로고    scopus 로고
    • Differential regulation of CFTRDeltaF508 degradation by ubiquitin ligases gp78 and Hrd1
    • doi: 10.1016/j.biocel.2009.10.005
    • Ballar P, Ors AU, Yang H, Fang S, (2010) Differential regulation of CFTRDeltaF508 degradation by ubiquitin ligases gp78 and Hrd1. Int J Biochem Cell Biol 42: 167-173. doi:10.1016/j.biocel.2009.10.005. PubMed: 19828134.
    • (2010) Int J Biochem Cell Biol , vol.42 , pp. 167-173
    • Ballar, P.1    Ors, A.U.2    Yang, H.3    Fang, S.4
  • 18
    • 0036479131 scopus 로고    scopus 로고
    • A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expression
    • doi: 10.1074/jbc.M110177200
    • Cheng J, Moyer BD, Milewski M, Loffing J, Ikeda M, et al. (2002) A Golgi-associated PDZ domain protein modulates cystic fibrosis transmembrane regulator plasma membrane expression. J Biol Chem 277: 3520-3529. doi:10.1074/jbc.M110177200. PubMed: 11707463.
    • (2002) J Biol Chem , vol.277 , pp. 3520-3529
    • Cheng, J.1    Moyer, B.D.2    Milewski, M.3    Loffing, J.4    Ikeda, M.5
  • 19
    • 0347717877 scopus 로고    scopus 로고
    • Modulation of mature cystic fibrosis transmembrane regulator protein by the PDZ domain protein CAL
    • doi: 10.1074/jbc.M308640200
    • Cheng J, Wang H, Guggino WB, (2004) Modulation of mature cystic fibrosis transmembrane regulator protein by the PDZ domain protein CAL. J Biol Chem 279: 1892-1898. doi:10.1074/jbc.M308640200. PubMed: 14570915.
    • (2004) J Biol Chem , vol.279 , pp. 1892-1898
    • Cheng, J.1    Wang, H.2    Guggino, W.B.3
  • 20
    • 34247258972 scopus 로고    scopus 로고
    • Targeting CAL as a negative regulator of DeltaF508-CFTR cell-surface expression: an RNA interference and structure-based mutagenetic approach
    • doi: 10.1074/jbc.M611049200
    • Wolde M, Fellows A, Cheng J, Kivenson A, Coutermarsh B, et al. (2007) Targeting CAL as a negative regulator of DeltaF508-CFTR cell-surface expression: an RNA interference and structure-based mutagenetic approach. J Biol Chem 282: 8099-8109. doi:10.1074/jbc.M611049200. PubMed: 17158866.
    • (2007) J Biol Chem , vol.282 , pp. 8099-8109
    • Wolde, M.1    Fellows, A.2    Cheng, J.3    Kivenson, A.4    Coutermarsh, B.5
  • 21
    • 77950649805 scopus 로고    scopus 로고
    • Syntaxin 6 and CAL mediate the degradation of the cystic fibrosis transmembrane conductance regulator
    • doi: 10.1091/mbc.E09-03-0229
    • Cheng J, Cebotaru V, Cebotaru L, Guggino WB, (2010) Syntaxin 6 and CAL mediate the degradation of the cystic fibrosis transmembrane conductance regulator. Mol Biol Cell 21: 1178-1187. doi:10.1091/mbc.E09-03-0229. PubMed: 20130090.
    • (2010) Mol Biol Cell , vol.21 , pp. 1178-1187
    • Cheng, J.1    Cebotaru, V.2    Cebotaru, L.3    Guggino, W.B.4
  • 22
    • 78650261973 scopus 로고    scopus 로고
    • A stabilizing influence: CAL PDZ inhibition extends the half-life of DeltaF508-CFTR
    • doi: 10.1002/anie.201005585
    • Cushing PR, Vouilleme L, Pellegrini M, Boisguerin P, Madden DR, (2010) A stabilizing influence: CAL PDZ inhibition extends the half-life of DeltaF508-CFTR. Angew Chem Int Ed Engl 49: 9907-9911. doi:10.1002/anie.201005585. PubMed: 21105033.
    • (2010) Angew Chem Int Ed Engl , vol.49 , pp. 9907-9911
    • Cushing, P.R.1    Vouilleme, L.2    Pellegrini, M.3    Boisguerin, P.4    Madden, D.R.5
  • 23
    • 79955662464 scopus 로고    scopus 로고
    • Crystallization and preliminary diffraction analysis of the CAL PDZ domain in complex with a selective peptide inhibitor
    • doi: 10.1107/S1744309111009985
    • Amacher JF, Cushing PR, Weiner JA, Madden DR, (2011) Crystallization and preliminary diffraction analysis of the CAL PDZ domain in complex with a selective peptide inhibitor. Acta Crystallogr Sect F Struct Biol Cryst Commun 67: 600-603. doi:10.1107/S1744309111009985.
    • (2011) Acta Crystallogr Sect F Struct Biol Cryst Commun , vol.67 , pp. 600-603
    • Amacher, J.F.1    Cushing, P.R.2    Weiner, J.A.3    Madden, D.R.4
  • 24
    • 16344381891 scopus 로고    scopus 로고
    • MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking
    • doi: 10.1091/mbc.E04-03-0216
    • Nakamura N, Fukuda H, Kato A, Hirose S, (2005) MARCH-II is a syntaxin-6-binding protein involved in endosomal trafficking. Mol Biol Cell 16: 1696-1710. doi:10.1091/mbc.E04-03-0216. PubMed: 15689499.
    • (2005) Mol Biol Cell , vol.16 , pp. 1696-1710
    • Nakamura, N.1    Fukuda, H.2    Kato, A.3    Hirose, S.4
  • 25
    • 32944455458 scopus 로고    scopus 로고
    • MARCH-III Is a novel component of endosomes with properties similar to those of MARCH-II
    • doi: 10.1093/jb/mvj012
    • Fukuda H, Nakamura N, Hirose S, (2006) MARCH-III Is a novel component of endosomes with properties similar to those of MARCH-II. J Biochem 139: 137-145. doi:10.1093/jb/mvj012. PubMed: 16428329.
    • (2006) J Biochem , vol.139 , pp. 137-145
    • Fukuda, H.1    Nakamura, N.2    Hirose, S.3
  • 26
    • 26244468727 scopus 로고    scopus 로고
    • Downregulation of cell surface receptors by the K3 family of viral and cellular ubiquitin E3 ligases
    • doi: 10.1111/j.0105-2896.2005.00314.x
    • Lehner PJ, Hoer S, Dodd R, Duncan LM, (2005) Downregulation of cell surface receptors by the K3 family of viral and cellular ubiquitin E3 ligases. Immunol Rev 207: 112-125. doi:10.1111/j.0105-2896.2005.00314.x. PubMed: 16181331.
    • (2005) Immunol Rev , vol.207 , pp. 112-125
    • Lehner, P.J.1    Hoer, S.2    Dodd, R.3    Duncan, L.M.4
  • 27
    • 0034748469 scopus 로고    scopus 로고
    • MHC class I ubiquitination by a viral PHD/LAP finger protein
    • doi: 10.1016/S1074-7613(01)00213-8
    • Boname JM, Stevenson PG, (2001) MHC class I ubiquitination by a viral PHD/LAP finger protein. Immunity 15: 627-636. doi:10.1016/S1074-7613(01)00213-8. PubMed: 11672544.
    • (2001) Immunity , vol.15 , pp. 627-636
    • Boname, J.M.1    Stevenson, P.G.2
  • 28
    • 0035945349 scopus 로고    scopus 로고
    • A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition
    • doi: 10.1083/jcb.200111010
    • Coscoy L, Sanchez DJ, Ganem D, (2001) A novel class of herpesvirus-encoded membrane-bound E3 ubiquitin ligases regulates endocytosis of proteins involved in immune recognition. J Cell Biol 155: 1265-1273. doi:10.1083/jcb.200111010. PubMed: 11756476.
    • (2001) J Cell Biol , vol.155 , pp. 1265-1273
    • Coscoy, L.1    Sanchez, D.J.2    Ganem, D.3
  • 29
    • 67349172917 scopus 로고    scopus 로고
    • The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases
    • doi: 10.1016/j.yexcr.2008.10.026
    • Nathan JA, Lehner PJ, (2009) The trafficking and regulation of membrane receptors by the RING-CH ubiquitin E3 ligases. Exp Cell Res 315: 1593-1600. doi:10.1016/j.yexcr.2008.10.026. PubMed: 19013150.
    • (2009) Exp Cell Res , vol.315 , pp. 1593-1600
    • Nathan, J.A.1    Lehner, P.J.2
  • 30
    • 0346373729 scopus 로고    scopus 로고
    • Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins
    • doi: 10.1128/JVI.78.3.1109-1120.2004
    • Bartee E, Mansouri M, Hovey Nerenberg BT, Gouveia K, Früh K, (2004) Downregulation of major histocompatibility complex class I by human ubiquitin ligases related to viral immune evasion proteins. J Virol 78: 1109-1120. doi:10.1128/JVI.78.3.1109-1120.2004. PubMed: 14722266.
    • (2004) J Virol , vol.78 , pp. 1109-1120
    • Bartee, E.1    Mansouri, M.2    Hovey Nerenberg, B.T.3    Gouveia, K.4    Früh, K.5
  • 31
    • 42149179893 scopus 로고    scopus 로고
    • MHC class II stabilization at the surface of human dendritic cells is the result of maturation-dependent MARCH I down-regulation
    • doi: 10.1073/pnas.0708874105
    • De Gassart A, Camosseto V, Thibodeau J, Ceppi M, Catalan N, et al. (2008) MHC class II stabilization at the surface of human dendritic cells is the result of maturation-dependent MARCH I down-regulation. Proc Natl Acad Sci U S A 105: 3491-3496. doi:10.1073/pnas.0708874105. PubMed: 18305173.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 3491-3496
    • De Gassart, A.1    Camosseto, V.2    Thibodeau, J.3    Ceppi, M.4    Catalan, N.5
  • 32
    • 65449174924 scopus 로고    scopus 로고
    • The HLA-DRalpha chain is modified by polyubiquitination
    • 19117940
    • Lapaque N, Jahnke M, Trowsdale J, Kelly AP, (2009) The HLA-DRalpha chain is modified by polyubiquitination. J Biol Chem 284: 7007-7016. PubMed: 19117940.
    • (2009) J Biol Chem , vol.284 , pp. 7007-7016
    • Lapaque, N.1    Jahnke, M.2    Trowsdale, J.3    Kelly, A.P.4
  • 33
    • 80054829298 scopus 로고    scopus 로고
    • Ubiquitin-mediated regulation of CD86 protein expression by the ubiquitin ligase membrane-associated RING-CH-1 (MARCH1)
    • doi: 10.1074/jbc.M110.204040
    • Corcoran K, Jabbour M, Bhagwandin C, Deymier MJ, Theisen DL, et al. (2011) Ubiquitin-mediated regulation of CD86 protein expression by the ubiquitin ligase membrane-associated RING-CH-1 (MARCH1). J Biol Chem 286: 37168-37180. doi:10.1074/jbc.M110.204040. PubMed: 21896490.
    • (2011) J Biol Chem , vol.286 , pp. 37168-37180
    • Corcoran, K.1    Jabbour, M.2    Bhagwandin, C.3    Deymier, M.J.4    Theisen, D.L.5
  • 34
    • 84871997357 scopus 로고    scopus 로고
    • MARCH2 promotes endocytosis and lysosomal sorting of carvedilol-bound β(2)-adrenergic receptors
    • doi: 10.1083/jcb.201208192
    • Han SO, Xiao K, Kim J, Wu JH, Wisler JW, et al. (2012) MARCH2 promotes endocytosis and lysosomal sorting of carvedilol-bound β(2)-adrenergic receptors. J Cell Biol 199: 817-830. doi:10.1083/jcb.201208192. PubMed: 23166351.
    • (2012) J Cell Biol , vol.199 , pp. 817-830
    • Han, S.O.1    Xiao, K.2    Kim, J.3    Wu, J.H.4    Wisler, J.W.5
  • 35
    • 0028027308 scopus 로고
    • Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain
    • doi: 10.1016/S0092-8674(94)90502-9
    • Treier M, Staszewski LM, Bohmann D, (1994) Ubiquitin-dependent c-Jun degradation in vivo is mediated by the delta domain. Cell 78: 787-798. doi:10.1016/S0092-8674(94)90502-9. PubMed: 8087846.
    • (1994) Cell , vol.78 , pp. 787-798
    • Treier, M.1    Staszewski, L.M.2    Bohmann, D.3
  • 36
    • 0032080043 scopus 로고    scopus 로고
    • Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR)
    • doi: 10.1016/S0014-5793(98)00402-5
    • Wang S, Raab RW, Schatz PJ, Guggino WB, Li M, (1998) Peptide binding consensus of the NHE-RF-PDZ1 domain matches the C-terminal sequence of cystic fibrosis transmembrane conductance regulator (CFTR). FEBS Lett 427: 103-108. doi:10.1016/S0014-5793(98)00402-5. PubMed: 9613608.
    • (1998) FEBS Lett , vol.427 , pp. 103-108
    • Wang, S.1    Raab, R.W.2    Schatz, P.J.3    Guggino, W.B.4    Li, M.5
  • 37
    • 0032555156 scopus 로고    scopus 로고
    • A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins
    • doi: 10.1073/pnas.95.15.8496
    • Hall RA, Ostedgaard LS, Premont RT, Blitzer JT, Rahman N, et al. (1998) A C-terminal motif found in the beta2-adrenergic receptor, P2Y1 receptor and cystic fibrosis transmembrane conductance regulator determines binding to the Na+/H+ exchanger regulatory factor family of PDZ proteins. Proc Natl Acad Sci U S A 95: 8496-8501. doi:10.1073/pnas.95.15.8496. PubMed: 9671706.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 8496-8501
    • Hall, R.A.1    Ostedgaard, L.S.2    Premont, R.T.3    Blitzer, J.T.4    Rahman, N.5
  • 38
    • 0032584744 scopus 로고    scopus 로고
    • An apical PDZ protein anchors the cystic fibrosis transmembrane conductance regulator to the cytoskeleton
    • doi: 10.1074/jbc.273.31.19797
    • Short DB, Trotter KW, Reczek D, Kreda SM, Bretscher A, et al. (1998) An apical PDZ protein anchors the cystic fibrosis transmembrane conductance regulator to the cytoskeleton. J Biol Chem 273: 19797-19801. doi:10.1074/jbc.273.31.19797. PubMed: 9677412.
    • (1998) J Biol Chem , vol.273 , pp. 19797-19801
    • Short, D.B.1    Trotter, K.W.2    Reczek, D.3    Kreda, S.M.4    Bretscher, A.5
  • 39
    • 33746878216 scopus 로고    scopus 로고
    • Identification of a PDZ protein, PIST, as a binding partner for Rho effector Rhotekin: biochemical and cell-biological characterization of Rhotekin-PIST interaction
    • doi: 10.1042/BJ20052015
    • Ito H, Iwamoto I, Morishita R, Nozawa Y, Asano T, et al. (2006) Identification of a PDZ protein, PIST, as a binding partner for Rho effector Rhotekin: biochemical and cell-biological characterization of Rhotekin-PIST interaction. Biochem J 397: 389-398. doi:10.1042/BJ20052015. PubMed: 16646955.
    • (2006) Biochem J , vol.397 , pp. 389-398
    • Ito, H.1    Iwamoto, I.2    Morishita, R.3    Nozawa, Y.4    Asano, T.5
  • 40
    • 0035800743 scopus 로고    scopus 로고
    • Association of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6
    • doi: 10.1074/jbc.M104137200
    • Charest A, Lane K, McMahon K, Housman DE, (2001) Association of a novel PDZ domain-containing peripheral Golgi protein with the Q-SNARE (Q-soluble N-ethylmaleimide-sensitive fusion protein (NSF) attachment protein receptor) protein syntaxin 6. J Biol Chem 276: 29456-29465. doi:10.1074/jbc.M104137200. PubMed: 11384996.
    • (2001) J Biol Chem , vol.276 , pp. 29456-29465
    • Charest, A.1    Lane, K.2    McMahon, K.3    Housman, D.E.4
  • 41
    • 13544273548 scopus 로고    scopus 로고
    • Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10
    • 15546864
    • Cheng J, Wang H, Guggino WB, (2005) Regulation of cystic fibrosis transmembrane regulator trafficking and protein expression by a Rho family small GTPase TC10. J Biol Chem 280: 3731-3739. PubMed: 15546864.
    • (2005) J Biol Chem , vol.280 , pp. 3731-3739
    • Cheng, J.1    Wang, H.2    Guggino, W.B.3
  • 42
    • 0025242929 scopus 로고
    • Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis
    • doi: 10.1016/0092-8674(90)90148-8
    • Cheng SH, Gregory RJ, Marshall J, Paul S, Souza DW, et al. (1990) Defective intracellular transport and processing of CFTR is the molecular basis of most cystic fibrosis. Cell 63: 827-834. doi:10.1016/0092-8674(90)90148-8. PubMed: 1699669.
    • (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
  • 43
    • 0027448163 scopus 로고
    • Spectrum of mutations in cystic fibrosis
    • doi: 10.1007/BF00768062
    • Cutting GR, (1993) Spectrum of mutations in cystic fibrosis. J Bioenerg Biomembr 25: 7-10. doi:10.1007/BF00768062. PubMed: 7680032.
    • (1993) J Bioenerg Biomembr , vol.25 , pp. 7-10
    • Cutting, G.R.1
  • 44
    • 0027162649 scopus 로고
    • Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis
    • doi: 10.1016/0092-8674(93)90353-R
    • Welsh MJ, Smith AE, (1993) Molecular mechanisms of CFTR chloride channel dysfunction in cystic fibrosis. Cell 73: 1251-1254. doi:10.1016/0092-8674(93)90353-R. PubMed: 7686820.
    • (1993) Cell , vol.73 , pp. 1251-1254
    • Welsh, M.J.1    Smith, A.E.2
  • 45
    • 24644464284 scopus 로고    scopus 로고
    • Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by high-throughput screening
    • doi: 10.1172/JCI24898
    • Pedemonte N, Lukacs GL, Du K, Caci E, Zegarra-Moran O, et al. (2005) Small-molecule correctors of defective DeltaF508-CFTR cellular processing identified by high-throughput screening. J Clin Invest 115: 2564-2571. doi:10.1172/JCI24898. PubMed: 16127463.
    • (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
  • 46
    • 33744831154 scopus 로고    scopus 로고
    • Rescue of DeltaF508-CFTR trafficking and gating in human cystic fibrosis airway primary cultures by small molecules
    • doi: 10.1152/ajplung.00169.2005
    • Van Goor F, Straley KS, Cao D, González J, Hadida S, et al. (2006) Rescue of DeltaF508-CFTR trafficking and gating in human cystic fibrosis airway primary cultures by small molecules. Am J Physiol Lung Cell Mol Physiol 290: L1117-L1130. doi:10.1152/ajplung.00169.2005. PubMed: 16443646.
    • (2006) Am J Physiol Lung Cell Mol Physiol , vol.290
    • Van Goor, F.1    Straley, K.S.2    Cao, D.3    González, J.4    Hadida, S.5
  • 47
    • 81755163563 scopus 로고    scopus 로고
    • Correction of the F508del-CFTR protein processing defect in vitro by the investigational drug VX-809
    • doi: 10.1073/pnas.1105787108
    • Van Goor F, Hadida S, Grootenhuis PD, Burton B, Stack JH, et al. (2011) Correction of the F508del-CFTR protein processing defect in vitro by the investigational drug VX-809. Proc Natl Acad Sci U S A 108: 18843-18848. doi:10.1073/pnas.1105787108. PubMed: 21976485.
    • (2011) Proc Natl Acad Sci U S A , vol.108 , pp. 18843-18848
    • Van Goor, F.1    Hadida, S.2    Grootenhuis, P.D.3    Burton, B.4    Stack, J.H.5
  • 48
    • 77952399647 scopus 로고    scopus 로고
    • Correction of the Delta phe508 cystic fibrosis transmembrane conductance regulator trafficking defect by the bioavailable compound glafenine
    • doi: 10.1124/mol.109.062679
    • Robert R, Carlile GW, Liao J, Balghi H, Lesimple P, et al. (2010) Correction of the Delta phe508 cystic fibrosis transmembrane conductance regulator trafficking defect by the bioavailable compound glafenine. Mol Pharmacol 77: 922-930. doi:10.1124/mol.109.062679. PubMed: 20200141.
    • (2010) Mol Pharmacol , vol.77 , pp. 922-930
    • Robert, R.1    Carlile, G.W.2    Liao, J.3    Balghi, H.4    Lesimple, P.5
  • 49
    • 80455162465 scopus 로고    scopus 로고
    • A CFTR potentiator in patients with cystic fibrosis and the G551D mutation
    • doi: 10.1056/NEJMoa1105185
    • Ramsey BW, Davies J, McElvaney NG, Tullis E, Bell SC, et al. (2011) A CFTR potentiator in patients with cystic fibrosis and the G551D mutation. N Engl J Med 365: 1663-1672. doi:10.1056/NEJMoa1105185. PubMed: 22047557.
    • (2011) N Engl J Med , vol.365 , pp. 1663-1672
    • Ramsey, B.W.1    Davies, J.2    McElvaney, N.G.3    Tullis, E.4    Bell, S.C.5
  • 50
    • 84855202429 scopus 로고    scopus 로고
    • Results of a phase IIa study of VX-809, an investigational CFTR corrector compound, in subjects with cystic fibrosis homozygous for the F508del-CFTR mutation
    • doi: 10.1136/thoraxjnl-2011-200393
    • Clancy JP, Rowe SM, Accurso FJ, Aitken ML, Amin RS, et al. (2012) Results of a phase IIa study of VX-809, an investigational CFTR corrector compound, in subjects with cystic fibrosis homozygous for the F508del-CFTR mutation. Thorax 67: 12-18. doi:10.1136/thoraxjnl-2011-200393. PubMed: 21825083.
    • (2012) Thorax , vol.67 , pp. 12-18
    • Clancy, J.P.1    Rowe, S.M.2    Accurso, F.J.3    Aitken, M.L.4    Amin, R.S.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.