Lipid-Protein Interactions at the Nicotinic Acetylcholine Receptor
نویسندگان
چکیده
منابع مشابه
Lipid-protein interactions at the nicotinic acetylcholine receptor. A functional coupling between nicotinic receptors and phosphatidic acid-containing lipid bilayers.
The structural and functional properties of reconstituted nicotinic acetylcholine receptor membranes composed of phosphatidyl choline either with or without cholesterol and/or phosphatidic acid have been examined to test the hypothesis that receptor conformational equilibria are modulated by the physical properties of the surrounding lipid environment. Spectroscopic and chemical labeling data i...
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We tested the hypothesis that membrane lipid composition influences drug action at membrane proteins by studying local anesthetic action at the nicotinic acetylcholine receptor (nAChR). Infrared difference spectra show that concentrations of tetracaine consistent with binding to the ion channel (<50 microM) stabilize a resting-like state when the nAChR is reconstituted into phosphatidylcholine ...
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Jin Oshikawa,1 Yoshiyuki Toya,1 Takayuki Fujita,1 Masato Egawa,2 Junichi Kawabe,3 Satoshi Umemura,1 and Yoshihiro Ishikawa1,3 1Departments of Physiology and Medicine, Yokohama City University School of Medicine, and 2Department of Medical Pathophysiology, Yokohama City University College of Nursing, Yokohama 236-0004, Japan; and 3Cardiovascular Research Institute, Departments of Medicine and Ce...
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The properties of the channel of the purified acetylcholine receptor (AChR) were investigated after reconstitution in planar lipid bilayers . The time course of the agonist-induced conductance exhibits a transient peak that relaxes to a steady state value. The macroscopic steady state membrane conductance increases with agonist concentration, reaching saturation at 10-5 M for carbamylcholine (C...
متن کاملSite-specific mutations of nicotinic acetylcholine receptor at the lipid-protein interface dramatically alter ion channel gating.
The nicotinic acetylcholine receptor (nAChR) is a postsynaptic, integral membrane protein consisting of five subunits with a stoichiometry of <Xz13'Y& (Pradier and McNamee, 1991). cDNA cloning reveals that each subunit has four homologous hydrophobic segments (Ml, M2, M3, and M4) that are believed to span the lipid bilayer. There is strong evidence that M2 is the ion channel-lining domain, but ...
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ژورنال
عنوان ژورنال: Journal of Biological Chemistry
سال: 2002
ISSN: 0021-9258
DOI: 10.1074/jbc.m108341200