G-protein-coupled receptor heteromer dynamics

Vilardaga, Jean-Pierre; Agnati, Luigi F.; Fuxé, Kjell; Ciruela, Francisco

doi:10.1242/jcs.063354

Cited by 48 publications

(44 citation statements)

References 59 publications

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“…In the case of non-mammalian vertebrate species, which express several KissR types, formation of heterodimers may be hypothesized to occur as already shown for other GPCRs (Vilardaga et al 2010).…”

Section: Interaction and Evolution Of Kiss/kissr Pairsmentioning

confidence: 80%

MOLECULAR EVOLUTION OF GPCRS: Kisspeptin/kisspeptin receptors

Pasquier¹,

Kamech²,

Lafont³

et al. 2014

Journal of Molecular Endocrinology

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Following the discovery of kisspeptin (Kiss) and its receptor (GPR54 or KissR) in mammals, phylogenetic studies revealed up to three Kiss and four KissR paralogous genes in other vertebrates. The multiplicity of Kiss and KissR types in vertebrates probably originated from the two rounds of whole-genome duplication (1R and 2R) that occurred in early vertebrates. This review examines compelling recent advances on molecular diversity and phylogenetic evolution of vertebrate Kiss and KissR. It also addresses, from an evolutionary point of view, the issues of the structure-activity relationships and interaction of Kiss with KissR and of their signaling pathways. Independent gene losses, during vertebrate evolution, have shaped the repertoire of Kiss and KissR in the extant vertebrate species. In particular, there is no conserved combination of a given Kiss type with a KissR type, across vertebrate evolution. The striking conservation of the biologically active ten-amino-acid C-terminal sequence of all vertebrate kisspeptins, probably allowed this evolutionary flexibility of Kiss/KissR pairs. KissR mutations, responsible for hypogonadotropic hypogonadism in humans, mostly occurred at highly conserved amino acid positions among vertebrate KissR. This further highlights the key role of these amino acids in KissR function. In contrast, less conserved KissR regions, notably in the intracellular C-terminal domain, may account for differential intracellular signaling pathways between vertebrate KissR. Cross talk between evolutionary and biomedical studies should contribute to further understanding of the Kiss/KissR structure-activity relationships and biological functions.

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Section: Interaction and Evolution Of Kiss/kissr Pairsmentioning

confidence: 80%

MOLECULAR EVOLUTION OF GPCRS: Kisspeptin/kisspeptin receptors

Pasquier¹,

Kamech²,

Lafont³

et al. 2014

Journal of Molecular Endocrinology

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“…One major characteristic of both GPCR and tyrosine kinase receptor superfamilies is their ability to form multimeric complexes (homomers and heteromers) that differentially modulate discrete sets of signaling effectors upon activation by a given ligand (24,25). In line with this, AdipoR1 has been recently shown to form homodimers in epithelial cells, endothelial cells, and myocytes (26).…”

mentioning

confidence: 90%

Adiponectin Receptors Form Homomers and Heteromers Exhibiting Distinct Ligand Binding and Intracellular Signaling Properties

Almabouada

Díaz‐Ruiz

Rabanal-Ruíz

et al. 2013

Journal of Biological Chemistry

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Background: Adiponectin receptors (AdipoR1 and 2) mediate the effects of adiponectin, which possesses insulin sensitizing and anti-inflammatory properties. Results: AdipoRs organize into oligomers exhibiting distinct interaction and signaling properties. Conclusion:The cellular response to adiponectin depends on the specific AdipoR repertoire. Significance: To envisage novel therapeutic strategies, the capacity of AdipoRs to form oligomeric complexes must be taken into consideration.

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“…G-protein-coupled receptors (GPCRs) are the most likely candidates for luminal sensors, not only because they represent the largest receptor family and respond to a diverse array of ligands, but also due to the finding that in heterologous systems several members of the GPCR family respond to macronutrients. Moreover, it has been proposed that homo-or heterodimerization may even extend the response spectrum of the GPCRs (Vilardaga et al 2010). For some of the nutrientresponsive GPCRs, there is evidence that they are expressed in the intestinal mucosa (Wellendorph et al 2010).…”

Section: Chemosensory Mechanisms Of Intestinal Cellsmentioning

confidence: 99%

Gastrointestinal chemosensation: chemosensory cells in the alimentary tract

Breer

Eberle

Frick

et al. 2012

Histochem Cell Biol

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Sensing potentially beneficial or harmful constituents in the luminal content by specialized cells in the gastrointestinal mucosa is an essential prerequisite for governing digestive processes, initiating protective responses and regulating food intake. Until recently, it was poorly understood how the gastrointestinal tract senses and responds to nutrients and non-nutrients in the diet; however, the enormous progress in unraveling the molecular machinery underlying the responsiveness of gustatory cells in the lingual taste buds to these compounds has been an important starting point for studying intestinal chemosensation. Currently, the field of nutrient sensing in the gastrointestinal tract is evolving rapidly and is benefiting from the deorphanization of previously unliganded G-protein-coupled receptors which respond to important nutrients, such as protein degradation products and free fatty acids as well as from the FACS-assisted isolation of distinct cell populations. This review focuses on mechanisms and principles underlying the chemosensory responsiveness of the alimentary tract. It describes the cell types which might potentially contribute to chemosensation within the gut: cells that can operate as specialized sensors and transducers for luminal factors and which communicate information from the gut lumen by releasing paracrine or endocrine acting messenger molecules. Furthermore, it addresses the current knowledge regarding the expression and localization of molecular elements that may be part of the chemosensory machinery which render some of the mucosal cells responsive to constituents of the luminal content, concentrating on candidate receptors and transporters for sensing nutrients.

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G-protein-coupled receptor heteromer dynamics

Cited by 48 publications

References 59 publications

MOLECULAR EVOLUTION OF GPCRS: Kisspeptin/kisspeptin receptors

MOLECULAR EVOLUTION OF GPCRS: Kisspeptin/kisspeptin receptors

Adiponectin Receptors Form Homomers and Heteromers Exhibiting Distinct Ligand Binding and Intracellular Signaling Properties

Gastrointestinal chemosensation: chemosensory cells in the alimentary tract

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