title: Coupling of ATP hydrolysis with channel gating by purified, reconstituted CFTR.
abstract: The cystic fibrosis transmembrane conductance regulator (CFTR) is a chloride channel situated on the apical membrane of epithelial cells. Our recent studies of purified, reconstituted CFTR revealed that it also functions as an ATPase and that there may be coupling between ATP hydrolysis and channel gating. Both the ATP turnover rate and channel gating are slow, in the range of 0.2 to 1 s(-1), and both activities are suppressed in a disease-causing mutation situated in a putative nucleotide binding motif. Our future studies using purified protein will be directed toward understanding the structural basis and mechanism for coupling between hydrolysis and channel function.
authors.affiliation: Department of Physiology, University of Toronto, Canada.
authors.forename: C E
authors.initials: CE
authors.lastname: Bear
authors.forename: C
authors.initials: C
authors.lastname: Li
authors.forename: K
authors.initials: K
authors.lastname: Galley
authors.forename: Y
authors.initials: Y
authors.lastname: Wang
authors.forename: E
authors.initials: E
authors.lastname: Garami
authors.forename: M
authors.initials: M
authors.lastname: Ramjeesingh
mesh_terms: D000255:Adenosine Triphosphate / Q000378:metabolism*; D019005:Cystic Fibrosis Transmembrane Conductance Regulator / Q000302:isolation & purification* / Q000378:metabolism* / Q000502:physiology; D006801:Humans; D006868:Hydrolysis; D015640:Ion Channel Gating / Q000502:physiology*; D008954:Models, Biological
chemical_list: C505032:CFTR protein, human; D019005:Cystic Fibrosis Transmembrane Conductance Regulator; D000255:Adenosine Triphosphate