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Ca²⁺ Sensitivity of Anoctamin 6/TMEM16F Is Regulated by the Putative Ca²⁺-Binding Reservoir at the N-Terminal Domain.

ABSTRACT: Anoctamin 6/TMEM16F (ANO6) is a dual-function protein with Ca²⁺-activated ion channel and Ca²⁺-activated phospholipid scramblase activities, requiring a high intracellular Ca²⁺ concentration (e.g., half-maximal effective Ca²⁺ concentration [EC₅₀] of [Ca²⁺]i > 10 μM), and strong and sustained depolarization above 0 mV. Structural comparison with Anoctamin 1/TMEM16A (ANO1), a canonical Ca²⁺- activated chloride channel exhibiting higher Ca²⁺ sensitivity (EC₅₀ of 1 μM) than ANO6, suggested that a homologous Ca²⁺-transferring site in the N-terminal domain (Nt) might be responsible for the differential Ca²⁺ sensitivity and kinetics of activation between ANO6 and ANO1. To eluci

SUBMITTER: Roh JW

PROVIDER: S-EPMC7941003 | biostudies-literature | 2021 Feb

REPOSITORIES: biostudies-literature

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Ca²⁺ Sensitivity of Anoctamin 6/TMEM16F Is Regulated by the Putative Ca²⁺-Binding Reservoir at the N-Terminal Domain.

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Dataset Information

Ca2+ Sensitivity of Anoctamin 6/TMEM16F Is Regulated by the Putative Ca2+-Binding Reservoir at the N-Terminal Domain.

OmicsDI is part of the ELIXIR infrastructure

Tweets

Ca²⁺ Sensitivity of Anoctamin 6/TMEM16F Is Regulated by the Putative Ca²⁺-Binding Reservoir at the N-Terminal Domain.