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%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
• 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
• 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

authors

• Arreola Gómez Jorge
• Hartzell H.C.

publication date

• 2019-01-01

funding provided via

• Consejo Nacional de Ciencia y Tecnología, CONACYT: AR067786, EY0114852  Grant
• National Eye Institute, NEI: R01EY014852  Grant
• National Institute of Arthritis and Musculoskeletal and Skin Diseases, NIAMS: R01AR067786  Grant
• National Institute of General Medical Sciences, NIGMS: R01GM132598  Grant
• National Institutes of Health, NIH  Grant

published in

• Cell Calcium  Journal

keywords

• 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

Digital Object Identifier (DOI)

• 10.1016/j.ceca.2019.102103

PubMed ID

• 31683182

start page

end page

volume

• 84