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Do lipids show state-dependent affinity to the voltage-gated potassium channel KvAP? | LitMetric

Do lipids show state-dependent affinity to the voltage-gated potassium channel KvAP?

J Biol Chem

Groupe d'étude des protéines membranaires (GÉPROM), Université de Montréal, Montréal CH3C 3J7, Canada Physiology, From the Departments of Physics and

Published: June 2014

AI Article Synopsis

Article Abstract

As all integral membrane proteins, voltage-gated ion channels are embedded in a lipid matrix that regulates their channel behavior either by physicochemical properties or by direct binding. Because manipulation of the lipid composition in cells is difficult, we investigated the influence of different lipids on purified KvAP channels reconstituted in planar lipid bilayers of known composition. Lipids developed two distinct and independent effects on the KvAP channels; lipids interacting with the pore lowered the energy barriers for the final transitions, whereas voltage sensor-bound lipids shifted the midpoint of activation dependent on their electrostatic charge. Above all, the midpoint of activation was determined only by those lipids the channels came in contact with first after purification and can seemingly only be exchanged if the channel resides in the open state. The high affinity of the bound lipids to the binding site has implications not only on our understanding of the gating mechanism but also on the general experimental design of any lipid dependence study.

Download full-text PDF

Source
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC4047412PMC
http://dx.doi.org/10.1074/jbc.M113.537134DOI Listing

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