Family-B G-protein-coupled receptors.docVIP

/2001/2/12/reviews/3013.1 Protein family review Family-B G-protein-coupled receptors Anthony J Harmar Address: Department of Neuroscience, University of Edinburgh, 1 George Square, Edinburgh EH8 9JZ, UK. E-mail: Tony.Harmar@ed.ac.uk Published: 23 November 2001 GenomeBiology 2001, 2(12):reviews3013.1–3013.10 The electronic version of this article is the complete one and can be found online at /2001/2/12/reviews/3013 ? BioMed Central Ltd (Print ISSN 1465-6906; Online ISSN 1465-6914) Summary All G-protein-coupled receptors (GPCRs) share a common molecular architecture (with seven putative transmembrane segments) and a common signaling mechanism, in that they interact with G proteins (heterotrimeric GTPases) to regulate the synthesis of intracellular second messengers such as cyclic AMP, inositol phosphates, diacylglycerol and calcium ions. Historically, GPCRs have been classified into six families, which were thought to be unrelated; three of these are found in vertebrates. Recent work has identified several new GCPR families and suggested the possibility of a common evolutionary origin for all of them. Family B (the secretin-receptor family or ‘family 2’) of the GPCRs is a small but structurally and functionally diverse group of proteins that includes receptors for polypeptide hormones, molecules thought to mediate intercellular interactions at the plasma membrane and a group of Drosophila proteins that regulate stress responses and longevity. Family-B GPCRs have been found in all animal species investigated, including mammals, Caenorhabditis elegans and Drosophila melanogaster, but not in plants, fungi or prokaryotes. In this article, I describe the structures and functions of family-B GPCRs and propose a simplified nomenclature for these proteins. All G-protein-coupled receptors (GPCRs) are thought to have the same molecular architecture, consisting of seven transmembrane domains (