Coupling of ATP Hydrolysis with Channel Gating by Purified, Reconstituted CFTR |
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Authors: | Christine E Bear Canhui Li Kevin Galley Yanchun Wang Elizabeth Garami Mohabir Ramjeesingh |
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Institution: | (1) Department of Physiology, University of Toronto, Medical Sciences Building, 1 King's College Circle, Toronto, Canada;(2) Division of Cell Biology, Research Institute, Hospital for Sick Children, 555 University Avenue, Toronto, Canada |
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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. |
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Keywords: | Cystic fibrosis transmembrane conductance regulator (CFTR) chloride channel activity ATPase activity purified protein |
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