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

• Type of Material: Article
• Authors: Jorge Arreola, Univ Autonoma San Luis Potosi; Criss Hartzell Jr., Emory University
• Language: English
• Date: 2019-12-01
• Publisher: ELSEVIER SCI LTD
• Publication Version: Author Accepted Manuscript (After Peer Review)
• Copyright Statement: 2019
• License: Creative Commons Attribution-NonCommercial-NoDerivs 4.0 International
• Final Published Version (URL): http://dx.doi.org/10.1016/j.ceca.2019.102103
• Title of Journal or Parent Work: CELL CALCIUM
• Volume: 84
• Start Page: 102103
• End Page: 102103
• Grant/Funding Information: Thanks to Huanghe Yang, Son Le, and Steven Foltz for helpful comments. Research on ANO 1 channels is supported by grants FC 2016-01-1955 and 219949 from CONACYT, Mexico (JA) and by grants EY0114852, AR067786, and GM132598 from the National Institutes of Health (HCH).
• Keywords: Science & Technology; Ion channel gating; Phospholipids; Calcium; Anion channels; CHLORIDE CHANNELS; Life Sciences & Biomedicine; PIP2; Ion channel regulation; Cell Biology
• Research Categories: Biology, General; Biology, Cell

Abstract

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)P2). These recent studies show that upon Ca2+ binding, PI(4,5)P2 cooperates to maintain the conductive state of ANO1. PI(4,5)P2 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)P2 repertoire and a new dimension to ANO1 gating.