Abstract
Opioid receptors are seven-transmembrane domain receptors that couple to intracellular signaling molecules by activating heterotrimeric G proteins. However, the receptor and G protein do not function in isolation but their activities are modulated by several accessory and scaffolding proteins. Examples include arrestins, kinases, and regulators of G protein signaling proteins. Accessory proteins contribute to the observed potency and efficacy of agonists, but also to the direction of signaling and the phenomenon of biased agonism. This review will present current knowledge of such proteins and how they may provide targets for future drug design.
Keywords: Opioid receptors, regulator of G protein signaling proteins, arrestins, G protein-coupled receptor kinases, protein kinase C, biased agonism, drug discovery.
Current Pharmaceutical Design
Title:Opioid Receptor Interacting Proteins and the Control of Opioid Signaling
Volume: 19 Issue: 42
Author(s): Jennifer T. Lamberts and John R. Traynor
Affiliation:
Keywords: Opioid receptors, regulator of G protein signaling proteins, arrestins, G protein-coupled receptor kinases, protein kinase C, biased agonism, drug discovery.
Abstract: Opioid receptors are seven-transmembrane domain receptors that couple to intracellular signaling molecules by activating heterotrimeric G proteins. However, the receptor and G protein do not function in isolation but their activities are modulated by several accessory and scaffolding proteins. Examples include arrestins, kinases, and regulators of G protein signaling proteins. Accessory proteins contribute to the observed potency and efficacy of agonists, but also to the direction of signaling and the phenomenon of biased agonism. This review will present current knowledge of such proteins and how they may provide targets for future drug design.
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Cite this article as:
Lamberts T. Jennifer and Traynor R. John, Opioid Receptor Interacting Proteins and the Control of Opioid Signaling, Current Pharmaceutical Design 2013; 19 (42) . https://dx.doi.org/10.2174/138161281942140105160625
DOI https://dx.doi.org/10.2174/138161281942140105160625 |
Print ISSN 1381-6128 |
Publisher Name Bentham Science Publisher |
Online ISSN 1873-4286 |
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