Regulation of KCNQ/Kv7 family voltage-gated K channels by lipids.

Taylor KC, Sanders CR
Biochim Biophys Acta Biomembr. 2017 1859 (4): 586-597

PMID: 27818172 · PMCID: PMC5305565 · DOI:10.1016/j.bbamem.2016.10.023

Many years of studies have established that lipids can impact membrane protein structure and function through bulk membrane effects, by direct but transient annular interactions with the bilayer-exposed surface of protein transmembrane domains, and by specific binding to protein sites. Here, we focus on how phosphatidylinositol 4,5-bisphosphate (PIP) and polyunsaturated fatty acids (PUFAs) impact ion channel function and how the structural details of the interactions of these lipids with ion channels are beginning to emerge. We focus on the Kv7 (KCNQ) subfamily of voltage-gated K channels, which are regulated by both PIP and PUFAs and play a variety of important roles in human health and disease. This article is part of a Special Issue entitled: Lipid order/lipid defects and lipid-control of protein activity edited by Dirk Schneider.

Copyright © 2016 Elsevier B.V. All rights reserved.

MeSH Terms (16)

Amino Acid Sequence Binding Sites Cell Membrane Epilepsy, Benign Neonatal Fatty Acids, Unsaturated Hearing Loss, Bilateral Humans Hydrophobic and Hydrophilic Interactions KCNQ1 Potassium Channel Long QT Syndrome Membrane Lipids Models, Molecular Phosphatidylinositol 4,5-Diphosphate Protein Binding Protein Isoforms Protein Structure, Secondary

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