Mechanisms of Cross-Talk between G-Protein-Coupled Receptors

Neurosignals ◽  
2002 ◽  
Vol 11 (1) ◽  
pp. 45-57 ◽  
Author(s):  
Yolande Cordeaux ◽  
Stephen J. Hill
Keyword(s):  
G Protein ◽  
Cross Talk ◽  
G Protein Coupled Receptors ◽  
G Protein Coupled

scholarly journals Mechanisms of cross-talk between G-protein-coupled receptors resulting in enhanced release of intracellular Ca2+

2003 ◽  
Vol 374 (2) ◽  
pp. 281-296 ◽  
Author(s):  
Tim D. WERRY ◽  
Graeme F. WILKINSON ◽  
Gary B. WILLARS
Keyword(s):  
G Protein ◽  
Cross Talk ◽  
Cell Function ◽  
Feedback Regulation ◽  
G Protein Coupled Receptors ◽  
Negative Feedback Regulation ◽  
Cellular Processes ◽  
Heterologous Desensitization ◽  
G Protein Coupled

Alteration in [Ca2+]i (the intracellular concentration of Ca2+) is a key regulator of many cellular processes. To allow precise regulation of [Ca2+]i and a diversity of signalling by this ion, cells possess many mechanisms by which they are able to control [Ca2+]i both globally and at the subcellular level. Among these are many members of the superfamily of GPCRs (G-protein-coupled receptors), which are characterized by the presence of seven transmembrane domains. Typically, those receptors able to activate PLC (phospholipase C) enzymes cause release of Ca2+ from intracellular stores and influence Ca2+ entry across the plasma membrane. It has been well documented that Ca2+ signalling by one type of GPCR can be influenced by stimulation of a different type of GPCR. Indeed, many studies have demonstrated heterologous desensitization between two different PLC-coupled GPCRs. This is not surprising, given our current understanding of negative-feedback regulation and the likely shared components of the signalling pathway. However, there are also many documented examples of interactions between GPCRs, often coupling preferentially to different signalling pathways, which result in a potentiation of Ca2+ signalling. Such interactions have important implications for both the control of cell function and the interpretation of in vitro cell-based assays. However, there is currently no single mechanism that adequately accounts for all examples of this type of cross-talk. Indeed, many studies either have not addressed this issue or have been unable to determine the mechanism(s) involved. This review seeks to explore a range of possible mechanisms to convey their potential diversity and to provide a basis for further experimental investigation.

scholarly journals Basic Concepts in G-Protein-Coupled Receptor Homo- and Heterodimerization

2007 ◽  
Vol 7 ◽  
pp. 48-57 ◽  
Author(s):  
Rafael Franco ◽  
Vicent Casadó ◽  
Antoni Cortés ◽  
Carla Ferrada ◽  
Josefa Mallol ◽  
...  
Keyword(s):  
Central Nervous System ◽  
G Protein ◽  
Conformational Changes ◽  
Cross Talk ◽  
G Protein Coupled Receptors ◽  
Allosteric Modulators ◽  
New Concepts ◽  
Binding Data ◽  
Basic Concepts ◽  
G Protein Coupled

Until recently, heptahelical G-protein-coupled receptors (GPCRs) were considered to be expressed as monomers on the cell surface of neuronal and non-neuronal cells. It is now becoming evident that this view must be overtly changed since these receptors can form homodimers, heterodimers, and higher-order oligomers on the plasma membrane. Here we discuss some of the basics and some new concepts of receptor homo- and heteromerization. Dimers-oligomers modify pharmacology, trafficking, and signaling of receptors. First of all, GPCR dimers must be considered as the main molecules that are targeted by neurotransmitters or by drugs. Thus, binding data must be fitted to dimer-based models. In these models, it is considered that the conformational changes transmitted within the dimer molecule lead to cooperativity. Cooperativity must be taken into account in the binding of agonists-antagonists-drugs and also in the binding of the so-called allosteric modulators. Cooperativity results from the intramolecular cross-talk in the homodimer. As an intramolecular cross-talk in the heterodimer, the binding of one neurotransmitter to one receptor often affects the binding of the second neurotransmitter to the partner receptor. Coactivation of the two receptors in a heterodimer can change completely the signaling pathway triggered by the neurotransmitter as well as the trafficking of the receptors. Heterodimer-specific drugs or dual drugs able to activate the two receptors in the heterodimer simultaneously emerge as novel and promising drugs for a variety of central nervous system (CNS) therapeutic applications.

scholarly journals Cross-Talk Between Insulin Signaling and G Protein–Coupled Receptors

2017 ◽  
Vol 70 (2) ◽  
pp. 74-86 ◽  
Author(s):  
Qin Fu ◽  
Qian Shi ◽  
Toni M. West ◽  
Yang K. Xiang
Keyword(s):  
G Protein ◽  
Cross Talk ◽  
Insulin Signaling ◽  
G Protein Coupled Receptors ◽  
G Protein Coupled

scholarly journals Deciphering the Cross-Talk of the Prostaglandin G-Protein Coupled Receptors EP2 and EP4: From Molecular Insights to Novel Anti-Tumor Targets

2012 ◽  
Vol 102 (3) ◽  
pp. 517a
Author(s):  
Sandra de Keijzer ◽  
Samantha L. Schwartz ◽  
Mark M. Rasenick ◽  
Carl G. Figdor ◽  
Vinod Subramaniam ◽  
...  
Keyword(s):  
G Protein ◽  
Cross Talk ◽  
G Protein Coupled Receptors ◽  
The Cross ◽  
G Protein Coupled
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