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Peptide fragment of the m3 muscarinic acetylcholine receptor activates G q but not G i2
Author(s) -
Kubota Makoto,
Wakamatsu Kaori
Publication year - 2008
Publication title -
journal of peptide science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.475
H-Index - 66
eISSN - 1099-1387
pISSN - 1075-2617
DOI - 10.1002/psc.1034
Subject(s) - heterotrimeric g protein , muscarinic acetylcholine receptor , peptide , chemistry , g protein , gq alpha subunit , g protein coupled receptor , muscarinic acetylcholine receptor m3 , intracellular , receptor , helix (gastropod) , biochemistry , microbiology and biotechnology , biology , ecology , snail
G q , a heterotrimeric guanine nucleotide‐binding protein, plays important roles such as the regulation of calcium mobilization and cell proliferation. This protein is considered as a promising drug target for the treatment of cardiac hypertrophy. Selective activation of G q would be quite useful for analyzing the role of G q in signaling pathways. We synthesized m3i3c—a peptide with 16 amino acid residues that corresponds to the junction between the C ‐terminus of the third intracellular loop and the sixth transmembrane helix (TM‐VI) of human m3 muscarinic acetylcholine receptor, which couples to G q but not G i2 . At micromolar concentrations, this peptide was found to activate G q but not G i2 . This peptide is the first small compound that selectively activates G q but not G i2 . Copyright © 2008 European Peptide Society and John Wiley & Sons, Ltd.