| Literature DB >> 27818172 |
Keenan C Taylor1, Charles R Sanders2.
Abstract
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 (PIP2) 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 PIP2 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.Entities:
Keywords: Annular; Channel; KCNQ1; Kv7.1; Lipids; Membrane; PIP2; PUFA; Potassium; Voltage-gated
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Year: 2016 PMID: 27818172 PMCID: PMC5305565 DOI: 10.1016/j.bbamem.2016.10.023
Source DB: PubMed Journal: Biochim Biophys Acta Biomembr ISSN: 0005-2736 Impact factor: 3.747