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Article

How Phosphorylation and ATPase Activity Regulate Anion Flux though the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR).

The Journal of biological chemistry - 8 Jul 2016

Zwick Matthias, Esposito Cinzia, Hellstern Manuel, Seelig Anna

Abstract excerpt

The cystic fibrosis transmembrane conductance regulator (CFTR, ABCC7), mutations of which cause cystic fibrosis, belongs to the ATP-binding cassette (ABC) transporter family and works as a channel for small anions, such as chloride and bicarbonate. Anion channel activity is known to depend on phosphorylation by cAMP-dependent protein kinase A (PKA) and CFTR-ATPase activity. Whereas anion channel activity has been...

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Identifiers

PMID: 27226582
DOI: 10.1074/jbc.M116.721415
PMCID: PMC4938172

Genes

CFTR

Variants

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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How Phosphorylation and ATPase Activity Regulate Anion Flux though the Cystic Fibrosis Transmembrane Conductance Regulator (CFTR).PMID 27226582Read ↗

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The non-hydrolytic pathway of cystic fibrosis transmembrane conductance regulator ion channel gating.Semantic proximity Read ↗

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Dibasic phosphorylation sites in the R domain of CFTR have stimulatory and inhibitory effects on channel activation.Semantic proximity Read ↗

Dibasic protein kinase A sites regulate bursting rate and nucleotide sensitivity of the cystic fibrosis transmembrane conductance regulator chloride channel.Semantic proximity Read ↗

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