2007
DOI: 10.1016/j.jmb.2006.10.086
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Domain Interdependence in the Biosynthetic Assembly of CFTR

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Cited by 209 publications
(320 citation statements)
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References 43 publications
(60 reference statements)
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“…CFTR 1-1172 lacks NBD2 but folds to a conformation that passes ERQC and functions at the cell surface as a Cl Ϫ channel (Cui et al, 2007). Treatment of cells with CAS inhibits calnexin-dependent protein folding reactions (Hammond et al, 1994;Ellgaard and Helenius, 2003) and blocks calnexin binding to CFTR ( Figure 3D).…”
Section: Calnexin Promotes Interactions Between Msd1 and Msd2 Of Cftrmentioning
confidence: 99%
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“…CFTR 1-1172 lacks NBD2 but folds to a conformation that passes ERQC and functions at the cell surface as a Cl Ϫ channel (Cui et al, 2007). Treatment of cells with CAS inhibits calnexin-dependent protein folding reactions (Hammond et al, 1994;Ellgaard and Helenius, 2003) and blocks calnexin binding to CFTR ( Figure 3D).…”
Section: Calnexin Promotes Interactions Between Msd1 and Msd2 Of Cftrmentioning
confidence: 99%
“…F508 of CFTR is located on the solvent-exposed surface of NBD1 (Lewis et al, 2004;Thibodeau et al, 2005), and the crystal structures of bacterial ABC transporters suggest that it makes contacts with cytosolic surface loops on MSD2 that are critical for stabilization of CFTR structure (Dawson and Locher, 2006;Serohijos et al, 2008). This supposition is supported by the observation that the F508 mutation disrupts assembly of CFTR 1-1172 (Cui et al, 2007) and makes similar CFTR fragments susceptible to cotranslational recognition by the ER-associated ubiquitin ligase RMA1 (Younger et al, 2006). NBD2 is the last domain on CFTR that is synthesized, and its folding and assembly into a complex with aminoterminal regions of CFTR seems to be slow and thus occur posttranslationally (Du et al, 2005).…”
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confidence: 94%
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