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)P(2)). These recent studies show that upon Ca(2+) 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.