Molecular mechanisms of acetylcholine receptor-lipid interactions: from model membranes to human biology

Biophysics Reviews
John E Baenziger, Corrie J B daCosta

Abstract

Lipids are potent modulators of the Torpedo nicotinic acetylcholine receptor. Lipids influence nicotinic receptor function by allosteric mechanisms, stabilizing varying proportions of pre-existing resting, open, desensitized, and uncoupled conformations. Recent structures reveal that lipids could alter function by modulating transmembrane α-helix/α-helix packing, which in turn could alter the conformation of the allosteric interface that links the agonist-binding and transmembrane pore domains-this interface is essential in the coupling of agonist binding to channel gating. We discuss potential mechanisms by which lipids stabilize different conformational states in the context of the hypothesis that lipid-nicotinic receptor interactions modulate receptor function at biological synapses.

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Citations

Mar 7, 2013·The Journal of Biological Chemistry·Jonathan M LabriolaJohn E Baenziger
Sep 10, 2013·Nature Chemical Biology·Corrie J B daCostaJohn E Baenziger
Mar 1, 2017·Proceedings of the National Academy of Sciences of the United States of America·Michael HabeckSteven J D Karlish
Aug 13, 2013·Structure·Corrie J B daCosta, John E Baenziger

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