Reviews |
From the Department of Biology, Syracuse University, Syracuse, NY.
Correspondence to Gerda E. Breitwieser, PhD, Department of Biology, Syracuse University, 122 Lyman Hall, 108 College Place, Syracuse, NY 13244. E-mail gebreitw{at}syr.edu
This Review is part of a thematic series on Heterodimerization of Signaling Molecules, which includes the following articles:
Regulation of G ProteinCoupled Receptor Signaling by Scaffold Proteins
G ProteinCoupled Receptor Oligomerization: Implications for G Protein Activation and Cell Signaling
Multitasking RGS Protein in the Heart: The Next Therapeutic Target?
Gerda Breitwieser Editor
The cardiovascular system is richly endowed with G proteincoupled receptors (GPCRs), members of the largest family of plasma membrane-localized receptors. During the last 10 years, it has become increasingly clear that many, if not all, GPCRs function in oligomeric complexes, as either homo- or hetero-oligomers. This review explores the mechanistic implications of GPCR dimerization and/or oligomerization on receptor activation and interactions with G proteins. The effects of GPCR oligomerization on receptor pharmacology, GPCR-mediated signaling, and potential contributions to GPCR crosstalk will be considered in the context of receptors important in the cardiovascular system. Our evolving understanding of the structural and functional consequences of GPCR oligomerization may provide novel and more selective sites for pharmacological tuning of cardiovascular function.
Key Words: G proteincoupled receptors oligomerization heterodimerization signal transduction G protein activation
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