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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%27s cytosolic side. These findings add a new function to the PI(4,5)P2 repertoire and a new dimension to ANO1 gating. © 2019 Elsevier Ltd
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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%2b 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%27s cytosolic side. These findings add a new function to the PI(4,5)P2 repertoire and a new dimension to ANO1 gating. © 2019 Elsevier Ltd
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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%2b 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. © 2019 Elsevier Ltd
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