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Are nicotinic acetylcholine receptors coupled to G proteins?
Author(s) -
Kabbani Nadine,
Nordman Jacob C.,
Corgiat Brian A.,
Veltri Daniel P.,
Shehu Amarda,
Seymour Victoria A.,
Adams David J.
Publication year - 2013
Publication title -
bioessays
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.175
H-Index - 184
eISSN - 1521-1878
pISSN - 0265-9247
DOI - 10.1002/bies.201300082
Subject(s) - heterotrimeric g protein , nicotinic agonist , muscarinic acetylcholine receptor , metabotropic receptor , g protein , acetylcholine receptor , receptor , microbiology and biotechnology , ligand gated ion channel , chemistry , ion channel , acetylcholine , biology , neuroscience , biophysics , biochemistry , pharmacology , agonist
It was, until recently, accepted that the two classes of acetylcholine (ACh) receptors are distinct in an important sense: muscarinic ACh receptors signal via heterotrimeric GTP binding proteins (G proteins), whereas nicotinic ACh receptors (nAChRs) open to allow flux of Na + , Ca 2+ , and K + ions into the cell after activation. Here we present evidence of direct coupling between G proteins and nAChRs in neurons. Based on proteomic, biophysical, and functional evidence, we hypothesize that binding to G proteins modulates the activity and signaling of nAChRs in cells. It is important to note that while this hypothesis is new for the nAChR, it is consistent with known interactions between G proteins and structurally related ligand‐gated ion channels. Therefore, it underscores an evolutionarily conserved metabotropic mechanism of G protein signaling via nAChR channels. Also watch the Video Abstract .