ABCMdb

PMID: 8810276

Price MP, Ishihara H, Sheppard DN, Welsh MJ
Function of Xenopus cystic fibrosis transmembrane conductance regulator (CFTR) Cl channels and use of human-Xenopus chimeras to investigate the pore properties of CFTR.
J Biol Chem. 1996 Oct 11;271(41):25184-91., [PubMed]

Sentences

No. Mutations Sentence Comment

254 ABCC7 p.Asp836* 5) We have shown that a CFTR construct containing only MSD1, NBD1, and the R domain (D836X) could form a Cl- channel with relatively normal conductive and permeability properties, albeit the efficiency of production was greatly reduced and regulation was altered (29). Login to comment 260 ABCC7 p.Pro99Leu ABCC7 p.Lys335Glu In MSD1, two mutations (P99L and K335E) that alter both anion permeability and conductance have been identified (15, 30); these are conserved in human and Xenopus CFTR. Login to comment 263 ABCC7 p.Thr1134Phe First, the mutation T1134F decreases the single-channel conductance of CFTR (18). Login to comment 268 ABCC7 p.Arg117His Assignment of this region as an extracellular loop is based on recognition of this region by an extracellular antibody (31), by insertion of a site that becomes glycosylated (32), and by effect of external pH on the R117H variant (13). Login to comment 269 ABCC7 p.Arg117His We previously found that mutation of an adjacent residue (Arg117 mutated to His) did not alter anion permeability but did decrease single channel conductance and altered the response to changes in extracellular pH (13). Login to comment 270 ABCC7 p.Arg117His Our data also suggest that this region influenced the pattern of gating; hX1-6 showed a pattern of gating characterized by a shortened open time, similar to that found in the R117H mutant. Login to comment 273 ABCC7 p.Asp836* 5) We have shown that a CFTR construct containing only MSD1, NBD1, and the R domain (D836X) could form a Cl2 channel with relatively normal conductive and permeability properties, albeit the efficiency of production was greatly reduced and regulation was altered (29). Login to comment 278 ABCC7 p.Asp836* This speculation is also consistent with our previous studies of D836X (29). Login to comment 279 ABCC7 p.Pro99Leu ABCC7 p.Lys335Glu In MSD1, two mutations (P99L and K335E) that alter both anion permeability and conductance have been identified (15, 30); these are conserved in human and Xenopus CFTR. Login to comment 282 ABCC7 p.Thr1134Phe First, the mutation T1134F decreases the single-channel conductance of CFTR (18). Login to comment 287 ABCC7 p.Arg117His Assignment of this region as an extracellular loop is based on recognition of this region by an extracellular antibody (31), by insertion of a site that becomes glycosylated (32), and by effect of external pH on the R117H variant (13). Login to comment 288 ABCC7 p.Arg117His We previously found that mutation of an adjacent residue (Arg117 mutated to His) did not alter anion permeability but did decrease single channel conductance and altered the response to changes in extracellular pH (13). Login to comment 289 ABCC7 p.Arg117His Our data also suggest that this region influenced the pattern of gating; hX1-6 showed a pattern of gating characterized by a shortened open time, similar to that found in the R117H mutant. Login to comment 297 ABCC7 p.Asp836* This speculation is also consistent with our previous studies of D836X (29). Login to comment