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

  • Cell Calcium. 2019 Dec;84:102103. doi: 10.1016/j.ceca.2019.102103.
Jorge Arreola  1 ,  H Criss Hartzell  2
Affiliations
  • 1. Physics Institute, Universidad Autónoma de San Luis Potosí, Ave. Dr. M. Nava #6, San Luis Potosí, SLP 78290, Mexico. Electronic address: [email protected].
  • 2. Department of Cell Biology, Emory University School of Medicine, Atlanta, GA, 30322, United States. Electronic address: [email protected].
PMID: 31683182 DOI: 10.1016/j.ceca.2019.102103
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.

Keywords
Anion channels; Calcium; Ion channel gating; Ion channel regulation; Phospholipids.
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