title: Phosphoinositides regulate ion channels.
abstract: Phosphoinositides serve as signature motifs for different cellular membranes and often are required for the function of membrane proteins. Here, we summarize clear evidence supporting the concept that many ion channels are regulated by membrane phosphoinositides. We describe tools used to test their dependence on phosphoinositides, especially phosphatidylinositol 4,5-bisphosphate, and consider mechanisms and biological meanings of phosphoinositide regulation of ion channels. This lipid regulation can underlie changes of channel activity and electrical excitability in response to receptors. Since different intracellular membranes have different lipid compositions, the activity of ion channels still in transit towards their final destination membrane may be suppressed until they reach an optimal lipid environment. This article is part of a Special Issue entitled Phosphoinositides.
authors.affiliation: Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA 98195-7290, USA. Electronic address: hille@u.washington.edu.
authors.forename: Bertil
authors.initials: B
authors.lastname: Hille
authors.affiliation: Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA 98195-7290, USA. Electronic address: dickson2@u.washington.edu.
authors.forename: Eamonn J
authors.initials: EJ
authors.lastname: Dickson
authors.affiliation: Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA 98195-7290, USA. Electronic address: mkruse@u.washington.edu.
authors.forename: Martin
authors.initials: M
authors.lastname: Kruse
authors.affiliation: Department of Physiology and Biophysics, University of Washington School of Medicine, Seattle, WA 98195-7290, USA. Electronic address: vivas@u.washington.edu.
authors.forename: Oscar
authors.initials: O
authors.lastname: Vivas
authors.affiliation: Department of Brain Science, Daegu Gyeongbuk Institute of Science and Technology (DGIST), Daegu 711-873, Republic of Korea. Electronic address: bcsuh@dgist.ac.kr.
authors.forename: Byung-Chang
authors.initials: BC
authors.lastname: Suh
mesh_terms: D015220:Calcium Channels / Q000235:genetics / Q000378:metabolism*; D002462:Cell Membrane / Q000737:chemistry / Q000378:metabolism; D018118:Chloride Channels / Q000235:genetics / Q000378:metabolism*; D053503:Epithelial Sodium Channels / Q000235:genetics / Q000378:metabolism*; D005786:Gene Expression Regulation; D006801:Humans; D017136:Ion Transport; D019269:Phosphatidylinositol 4,5-Diphosphate / Q000378:metabolism*; D015221:Potassium Channels / Q000235:genetics / Q000378:metabolism*; D043562:Receptors, G-Protein-Coupled / Q000235:genetics / Q000378:metabolism; D015398:Signal Transduction; D050051:Transient Receptor Potential Channels / Q000235:genetics / Q000378:metabolism*; D010738:Type C Phospholipases / Q000235:genetics / Q000378:metabolism
chemical_list: D015220:Calcium Channels; D018118:Chloride Channels; D053503:Epithelial Sodium Channels; D019269:Phosphatidylinositol 4,5-Diphosphate; D015221:Potassium Channels; D043562:Receptors, G-Protein-Coupled; D050051:Transient Receptor Potential Channels; D010738:Type C Phospholipases
keywords: Calcium channel; G-protein coupled receptor (GPCR); Phosphatidylinositol 4,5-bisphosphate; Phospholipase C (PLC); Potassium channel; Transient receptor potential channel (TRP channel)