NDLI: A kinase-regulated mechanism controls CFTR channel gating by disrupting bivalent PDZ domain interactions.

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A kinase-regulated mechanism controls CFTR channel gating by disrupting bivalent PDZ domain interactions.

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A kinase-regulated mechanism controls CFTR channel gating by disrupting bivalent PDZ domain interactions.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Raghuram, Viswanathan Foskett, J. Kevin Hormuth, Hayley
Description	Author Affiliation: Raghuram V ( Department of Physiology, University of Pennsylvania, Philadelphia, PA 19104-6085, USA.);
Abstract	Dynamic regulation of ion channels is critical for maintaining fluid balance in epithelial tissues. Cystic fibrosis, a genetic disease characterized by impaired fluid transport in epithelial tissues, is caused by dysfunctional cystic fibrosis transmembrane conductance regulator (CFTR) Cl- channel activity. Recent studies have shown that binding of PSD-95/Dlg/ZO-1 (PDZ) domain proteins to CFTR is important for retaining it at the apical membrane and for regulating its channel activity. Here, we describe a phosphorylation mechanism that regulates CFTR channel activity, which is mediated by PDZ domains. The Na+/H+ exchanger regulatory factor (NHERF) binds to CFTR and increases its open probability (Po). Protein kinase C disrupts the stimulatory effect of NHERF on CFTR channel Po. Phosphorylation by PKC of Ser-162 in the PDZ2 domain of NHERF is critical for this functional effect. Furthermore, a mutation in PDZ2 that mimics phosphorylation decreases CFTR binding and disrupts the ability of NHERF PDZ1-2 to stimulate CFTR channel Po. Our results identify a role for PKC and suggest that phosphorylation of NHERF PDZ2 domain may be an important mechanism for regulating CFTR channel activity.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	16
Volume Number	100
Language	English
Publisher	National Academy of Sciences
Publisher Date	2003-08-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cystic Fibrosis Transmembrane Conductance Regulator Chemistry Metabolism Amino Acid Sequence Animals Aspartic Acid CHO Cells Cricetinae Cross-Linking Reagents Pharmacology Dose-Response Relationship, Drug Electrophysiology Epitopes Ions Molecular Sequence Data Mutation Nerve Tissue Proteins Phosphorylation Precipitin Tests Protein Kinase C Protein Structure, Tertiary Sequence Homology, Amino Acid Serine Signal Transduction Sodium-Hydrogen Antiporter Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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