Promiscuous Coupling at Receptor-Gα Fusion Proteins THE RECEPTOR OF ONE COVALENT COMPLEX INTERACTS WITH THE α-SUBUNIT OF ANOTHER
Paola Molinari,Caterina Ambrosio,Daniela Riitano,Maria Sbraccia,Maria Cristina Grò,Tommaso Costa +5 more
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TLDR
There is no entropy drive from the linked condition of fusion proteins and their signaling may result from the GPCR of one complex interacting with the α-subunit of another, suggesting that the enhanced coupling efficiency commonly observed for fusion proteins is not due to the receptor tether, but to the transmembrane helix that anchors Gα to the membrane.About:
This article is published in Journal of Biological Chemistry.The article was published on 2003-05-02 and is currently open access. It has received 56 citations till now. The article focuses on the topics: Fusion protein & G protein-coupled receptor.read more
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Allosteric communication between protomers of dopamine class A GPCR dimers modulates activation.
TL;DR: A functional complementation assay is developed that enables control of the identity of the components comprising the signaling unit and makes possible the characterization of signaling from a defined heterodimer unit.
Journal ArticleDOI
Methods to monitor the quaternary structure of G protein-coupled receptors.
Graeme Milligan,Michel Bouvier +1 more
TL;DR: A wide range of approaches have been applied to examine the quaternary structure of G protein‐coupled receptors, the basis of such protein–protein interactions and how such interactions might modulate the pharmacology and function of these receptors, and their relative benefits and limitations are discussed.
Journal ArticleDOI
G-protein-coupled receptor heterodimers: pharmacology, function and relevance to drug discovery.
TL;DR: Differential pharmacology, function and regulation of GPCR hetero-dimers and -oligomers suggest means to selectively target GPCRs in different tissues and hint that the mechanism of function of several pharmacological agents might be different in vivo than anticipated from simple ligand-screening programmes that rely on heterologous expression of a single G PCR.
Journal ArticleDOI
Dimers of Class A G Protein-coupled Receptors Function via Agonist-mediated Trans-activation of Associated G Proteins
TL;DR: It is demonstrated that dimers of these class A receptors function via trans-activation of associated G proteins via transmembrane helix 1 in dimerization.
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The state of GPCR research in 2004
TL;DR: 20 questions of fundamental importance to the future development of the field are posed to 20 of the world's leading experts on GPCR research, and here are their replies.
References
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TL;DR: This approach provides two major advantages compared with other available methods: it uses an exact mathematical model of the ligand-binding system, thereby avoiding the possible biases introduced by several commonly used approximations and it uses a statistically valid, appropriately weighted least-squares curve-fitting algorithm with objective measurement of goodness of fit.
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G-protein-coupled receptor heterodimerization modulates receptor function
Bryen A. Jordan,Lakshmi A. Devi +1 more
TL;DR: In this article, the authors provide biochemical and pharmacological evidence for the heterodimerization of two fully functional opioid receptors, κ and δ, which results in a new receptor that exhibits ligand binding and functional properties that are distinct from those of either receptor.
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Enzyme changes in neonatal skeletal muscle: effect of thyroid deficiency
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Dimerization: an emerging concept for G protein-coupled receptor ontogeny and function.
TL;DR: The reports of heterodimerization between receptor subtypes suggest a potential level of receptor complexity that could account for previously unexpected pharmacological diversities and change views on the structure and activation processes of GPCRs.
Journal ArticleDOI
Membrane organization in G-protein mechanisms.
TL;DR: A full understanding of G‐protein‐coupled receptors must include a better description of the organization of these systems in cell membranes, which is likely to be more highly organized than previously appreciated.
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