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

被引：15
|
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.
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页数：4
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