Abstract
The adrenergic receptors are among the best characterized G protein-coupled receptors (GPCRs) and knowledge on this receptor family has provided several important paradigms about GPCR function and regulation. One of the most recent paradigms initially supported by studies on adrenergic receptors is that both βarrestins and G proteincoupled receptors themselves can act as scaffolds binding a variety of proteins and this can result in growing complexity of the receptor-mediated cellular effects. In this review we will briefly summarize the main features of βarrestin binding to the adrenergic receptor subtypes and we will review more in detail the main proteins found to selectively interact with distinct AR subtype. At the end, we will review the main findings on oligomerization of the AR subtypes.
Keywords: adrenergic receptor subtypes, signaling complexes, arrestins, receptor, oligomerization, protein-protein interactions, catecholamines, G protein coupled receptors, GPCR, beta-AR, receptor oligomerization
Current Drug Targets
Title: Protein-Protein Interactions at the Adrenergic Receptors
Volume: 13 Issue: 1
Author(s): Susanna Cotecchia, Laura Stanasila and Dario Diviani
Affiliation:
Keywords: adrenergic receptor subtypes, signaling complexes, arrestins, receptor, oligomerization, protein-protein interactions, catecholamines, G protein coupled receptors, GPCR, beta-AR, receptor oligomerization
Abstract: The adrenergic receptors are among the best characterized G protein-coupled receptors (GPCRs) and knowledge on this receptor family has provided several important paradigms about GPCR function and regulation. One of the most recent paradigms initially supported by studies on adrenergic receptors is that both βarrestins and G proteincoupled receptors themselves can act as scaffolds binding a variety of proteins and this can result in growing complexity of the receptor-mediated cellular effects. In this review we will briefly summarize the main features of βarrestin binding to the adrenergic receptor subtypes and we will review more in detail the main proteins found to selectively interact with distinct AR subtype. At the end, we will review the main findings on oligomerization of the AR subtypes.
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Cite this article as:
Cotecchia Susanna, Stanasila Laura and Diviani Dario, Protein-Protein Interactions at the Adrenergic Receptors, Current Drug Targets 2012; 13 (1) . https://dx.doi.org/10.2174/138945012798868489
DOI https://dx.doi.org/10.2174/138945012798868489 |
Print ISSN 1389-4501 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-5592 |
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