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First published online September 9, 2005

Journal of Cell Science 118, 1803e (2005)
© The Company of Biologists Limited
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In this issue

Channelled treatment for cystic fibrosis


In cystic fibrosis, the loss-of-function of CFTR, a membrane protein that allows apical efflux of Cl- from secretory epithelial cells, causes the mucus obstruction characteristic of the disease. The Cl- channel CIC-2 might function as an alternative route for Cl- efflux that, if pharmacologically activated, would compensate for CFTR deficiency, but its cellular localization is controversial. On p. 4243, Francisco Sepúlveda and co-workers use immunocytochemistry to show that CIC-2 localizes exclusively to the basolateral membranes of absorptive intestinal epithelial cells in vivo. Then, in transfection assays, they demonstrate that CIC-2 sorts to the basolateral membrane of several epithelial cell lines; this sorting is dependent on the AP-1B clathrin adaptor complex and on a di-leucine motif in a C-terminal crystathione beta synthase domain (CBS-2) of CIC-2. Drugs that modulate the function of the CBS-2 domain might therefore allow CIC-2 to compensate for loss of CFTR in cystic fibrosis by altering its targeting.


Related articles in JCS:

Basolateral localization of native ClC-2 chloride channels in absorptive intestinal epithelial cells and basolateral sorting encoded by a CBS-2 domain di-leucine motif
Gaspar Peña-Münzenmayer, Marcelo Catalán, Isabel Cornejo, Carlos D. Figueroa, James E. Melvin, María I. Niemeyer, L. Pablo Cid, and Francisco V. Sepúlveda
JCS 2005 118: 4243-4252. [Abstract] [Full Text]  




This Article
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