Wasted TMEM16A channels are rescued by phosphatidylinositol 4,5-bisphosphate
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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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Anion channels; Calcium; Ion channel gating; Ion channel regulation; Phospholipids anoctamin 1; calcium ion; dimer; phosphatidylinositol 4,5 bisphosphate; anoctamin 1; calcium; phosphatidylinositol 4,5 bisphosphate; Article; binding site; calcium binding; channel gating; cytoplasm; cytosol; mutation; nonhuman; priority journal; protein conformation; protein expression; protein structure; regulatory mechanism; animal; calcium signaling; channel gating; cytoskeleton; genetics; human; metabolism; Animals; Anoctamin-1; Calcium; Calcium Signaling; Cytoskeleton; Cytosol; Humans; Ion Channel Gating; Phosphatidylinositol 4,5-Diphosphate
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