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Article

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

Proceedings of the National Academy of Sciences of the United States of America - 5 Aug 2003

Raghuram Viswanathan, Hormuth Hayley, Foskett J Kevin

Abstract excerpt

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...

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Identifiers

PMID: 12881487
DOI: 10.1073/pnas.1633250100
PMCID: PMC170967

Genes

CFTR
PSD

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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A kinase-regulated mechanism controls CFTR channel gating by disrupting bivalent PDZ domain interactions.PMID 12881487Read ↗

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The role of the C terminus and Na+/H+ exchanger regulatory factor in the functional expression of cystic fibrosis transmembrane conductance regulator in nonpolarized cells and epithelia.Semantic proximity Read ↗

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The Relative Binding Affinities of PDZ Partners for CFTR: A Biochemical Basis for Efficient Endocytic RecyclingSemantic proximity Read ↗

Protein kinase D-mediated phosphorylation of polycystin-2 (TRPP2) is essential for its effects on cell growth and calcium channel activity.Semantic proximity Read ↗

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Inhibition of protein kinase CK2 closes the CFTR Cl channel, but has no effect on the cystic fibrosis mutant deltaF508-CFTR.Semantic proximity Read ↗

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