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Allosteric modulation of M1 muscarinic acetylcholine receptor internalization and subcellular trafficking

Yeatman, Holly R.; Lane, J. Robert; Choy, Kwok Ho Christopher; Lambert, Nevin A.; Sexton, Patrick M.; Christopoulos, Arthur; Canals, Meritxell

Authors

Holly R. Yeatman

J. Robert Lane

Kwok Ho Christopher Choy

Nevin A. Lambert

Patrick M. Sexton

Arthur Christopoulos



Abstract

Background: The effects of allosteric modulators on G protein-coupled receptor trafficking are largely unknown. Results: The allosteric ligand BQCA modulates M1 mAChR arrestin recruitment and receptor trafficking. Conclusion: M1 mAChR trafficking is arrestin- and G protein-dependent and modulated by BQCA. Significance: The impact of allosteric modulators on receptor trafficking needs to be assessed when considering this family of ligands as potential chronic therapies. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc. Published in the U.S.A.

Citation

Yeatman, H. R., Lane, J. R., Choy, K. H. C., Lambert, N. A., Sexton, P. M., Christopoulos, A., & Canals, M. (2014). Allosteric modulation of M1 muscarinic acetylcholine receptor internalization and subcellular trafficking. Journal of Biological Chemistry, 289(22), 15856-15866. https://doi.org/10.1074/jbc.M113.536672

Journal Article Type Article
Acceptance Date Apr 14, 2014
Online Publication Date May 30, 2014
Publication Date May 30, 2014
Deposit Date Jan 17, 2020
Journal Journal of Biological Chemistry
Print ISSN 0021-9258
Electronic ISSN 1083-351X
Publisher American Society for Biochemistry and Molecular Biology
Peer Reviewed Peer Reviewed
Volume 289
Issue 22
Pages 15856-15866
DOI https://doi.org/10.1074/jbc.M113.536672
Keywords Biochemistry; Biology; Allosteric modulation; Allosteric modulators; Arrestins; G protein coupled receptors; Muscarinic acetylcholine receptors; Receptor trafficking; Subcellular trafficking; Ligands; benzyl quinolone carboxylic acid; beta arrestin 1; bet
Public URL https://www.scopus.com/inward/record.uri?eid=2-s2.0-84901708225&doi=10.1074%2fjbc.M113.536672&partnerID=40&md5=7f6a1afd0afb36332ed8ae68dfee2d8e