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J Biol Chem, Vol. 274, Issue 12, 7627-7630, March 19, 1999

COMMUNICATION
A Single Conductance Pore for Chloride Ions Formed by Two Cystic Fibrosis Transmembrane Conductance Regulator Molecules

Bryan Zerhusen, Jiying Zhao, Junxia Xie, Pamela B. Davis, and Jianjie Ma

From the Departments of Physiology and Biophysics and  Pediatrics, Case Western Reserve University School of Medicine, Cleveland, Ohio 44106

The cystic fibrosis transmembrane conductance regulator (CFTR) is a cAMP-dependent protein kinase (PKA)- and ATP-regulated chloride channel, whose gating process involves intra- or intermolecular interactions among the cytosolic domains of the CFTR protein. Tandem linkage of two CFTR molecules produces a functional chloride channel with properties that are similar to those of the native CFTR channel, including trafficking to the plasma membrane, ATP- and PKA-dependent gating, and a unitary conductance of 8 picosiemens (pS). A heterodimer, consisting of a wild type and a mutant CFTR, also forms an 8-pS chloride channel with mixed gating properties of the wild type and mutant CFTR channels. The data suggest that two CFTR molecules interact together to form a single conductance pore for chloride ions.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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