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Biochim Biophys Acta Biomembr. 2017 Apr;1859(4):586-597. doi: 10.1016/j.bbamem.2016.10.023. Epub 2016 Nov 4.

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

Author information

1
Department of Biochemistry, Vanderbilt University, Nashville, TN, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN, USA.
2
Department of Biochemistry, Vanderbilt University, Nashville, TN, USA; Center for Structural Biology, Vanderbilt University, Nashville, TN, USA; Department of Medicine, Vanderbilt University Medical Center, Nashville, TN, USA. Electronic address: chuck.sanders@vanderbilt.edu.

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.

KEYWORDS:

Annular; Channel; KCNQ1; Kv7.1; Lipids; Membrane; PIP2; PUFA; Potassium; Voltage-gated

PMID:
27818172
PMCID:
PMC5305565
DOI:
10.1016/j.bbamem.2016.10.023
[Indexed for MEDLINE]
Free PMC Article

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