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MOLECULAR EVOLUTION OF GPCRS: Kisspeptin/kisspeptin receptors

Authors :
Jérémy Pasquier
Nédia Kamech
Karine Rousseau
Anne-Gaëlle Lafont
Hubert Vaudry
Sylvie Dufour
Biologie des Organismes et Ecosystèmes Aquatiques (BOREA)
Université de Caen Normandie (UNICAEN)
Normandie Université (NU)-Normandie Université (NU)-Muséum national d'Histoire naturelle (MNHN)-Institut de Recherche pour le Développement (IRD)-Sorbonne Université (SU)-Centre National de la Recherche Scientifique (CNRS)-Université des Antilles (UA)
Source :
Journal of Molecular Endocrinology, Journal of Molecular Endocrinology, BioScientifica, 2014, 52 (3), pp.T101-T117. ⟨10.1530/JME-13-0224⟩
Publication Year :
2014
Publisher :
Bioscientifica, 2014.

Abstract

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 ofKissandKissRin the extant vertebrate species. In particular, there is no conserved combination of a givenKisstype with aKissRtype, 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.

Details

ISSN :
14796813 and 09525041
Volume :
52
Database :
OpenAIRE
Journal :
Journal of Molecular Endocrinology
Accession number :
edsair.doi.dedup.....e8e63053f88e7b6faecd7ba69383cced