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Article

Acidic amino acids in the first intracellular loop contribute to voltage- and calcium- dependent gating of anoctamin1/TMEM16A.

PloS one - 1 Jan 2014

Xiao Qinghuan, Cui Yuanyuan

Abstract excerpt

Anoctamin1 (Ano1, or TMEM16A) is a Ca2+-activated chloride channel that is gated by both voltage and Ca2+. We have previously identified that the first intracellular loop that contains a high density of acidic residues mediates voltage- and calcium-dependent gating of Ano1. Mutation of the four consecutive glutamates (444EEEE447) inhibits the voltage-dependent activation of Ano1, whereas deletion of these...

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Identifiers

PMID: 24901998
DOI: 10.1371/journal.pone.0099376
PMCID: PMC4047086

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Source receipt: pubmed, retrieved 7 Sept 2026.

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Acidic amino acids in the first intracellular loop contribute to voltage- and calcium- dependent gating of anoctamin1/TMEM16A.PMID 24901998Read ↗

Explaining calcium-dependent gating of anoctamin-1 chloride channels requires a revised topology.Semantic proximity Read ↗

Voltage-Dependent Protonation of the Calcium Pocket Enable Activation of the Calcium-Activated Chloride Channel Anoctamin-1 (TMEM16A).Semantic proximity Read ↗

The voltage dependence of the TMEM16B/anoctamin2 calcium-activated chloride channel is modified by mutations in the first putative intracellular loop.Semantic proximity Read ↗

Two helices in the third intracellular loop determine anoctamin 1 (TMEM16A) activation by calcium.Semantic proximity Read ↗

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