| Asymmetry of GPCR oligomers supports their functional relevance. | |
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MedLine Citation:
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PMID: 21715028 Owner: NLM Status: Publisher |
Abstract/OtherAbstract:
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G protein-coupled receptors (GPCRs) can exist as dimers or as larger oligomeric clusters that enable intercommunication between different receptor protomers within the same complex. This phenomenon is observed at three distinct levels: (i) at the level of ligand binding where the activation of one protomer can allosterically inhibit or facilitate ligand binding to the second protomer; (ii) at the level of ligand-induced conformational switches, which occur between transmembrane domains of the two protomers; and (iii) within GPCR-associated protein complexes, either directly at the level of GPCR-interacting proteins or at further downstream levels of the complex. Intercommunication at these different levels introduces asymmetry within GPCR dimers wherein each protomer fulfills its specific task. In this review, we discuss how the asymmetric behavior of GPCRs highlights the advantage of oligomeric receptor organization and supports the functional relevance of GPCR dimerization. |
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Authors:
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Pascal Maurice; Maud Kamal; Ralf Jockers |
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Publication Detail:
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Type: JOURNAL ARTICLE Date: 2011-6-27 |
Journal Detail:
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Title: Trends in pharmacological sciences Volume: - ISSN: 1873-3735 ISO Abbreviation: - Publication Date: 2011 Jun |
Date Detail:
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Created Date: 2011-6-30 Completed Date: - Revised Date: - |
Medline Journal Info:
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Nlm Unique ID: 7906158 Medline TA: Trends Pharmacol Sci Country: - |
Other Details:
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Languages: ENG Pagination: - Citation Subset: - |
Copyright Information:
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Copyright © 2011. Published by Elsevier Ltd. |
Affiliation:
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Inserm, U1016, Institut Cochin, 22 rue Méchain, 75014 Paris, France; Centre National de la Recherche Scientifique, UMR 8104, Paris, France; Université Paris Descartes, Paris, France. |
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