Wasted TMEM16A channels are rescued by phosphatidylinositol 4,5-bisphosphate

被引：18

作者：

Arreola, Jorge ^{[1
]}

Hartzell, H. Criss ^{[2
]}

机构：

[1] Univ Autonoma San Luis Potosi, Phys Inst, Ave Dr M Nava 6, San Luis Potosi 78290, Slp, Mexico

[2] Emory Univ, Sch Med, Dept Cell Biol, Atlanta, GA 30322 USA

来源：

CELL CALCIUM | 2019年 / 84卷

基金：

美国国家卫生研究院;

关键词：

Phospholipids; Anion channels; Ion channel gating; Calcium; Ion channel regulation; CHLORIDE CHANNELS; PIP2;

D O I：

10.1016/j.ceca.2019.102103

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Recently there has been a flurry of interest in the regulation of the homo-dimeric calcium-activated chloride channel ANO1 (also known as TMEM16A) by phosphatidylinositol (4,5)-bisphosphate (PI(4,5)P-2). These recent studies show that upon Ca2+ binding, PI(4,5)P-2 cooperates to maintain the conductive state of ANO1. PI(4,5)P-2 does so by binding to sites or modules on the protein's cytosolic side. These findings add a new function to the PI (4,5)P-2 repertoire and a new dimension to ANO1 gating.

引用

页数：4

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