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New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors
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2014 (English)In: Annals of the New York Academy of Sciences, ISSN 0077-8923, E-ISSN 1749-6632, Vol. 1333, 43-64 p.Article in journal (Refereed) Published
Abstract [en]

The class of adhesion G protein-coupled receptors (aGPCRs), with 33 human homologs, is the second largest family of GPCRs. In addition to a seven-transmembrane α-helix-a structural feature of all GPCRs-the class of aGPCRs is characterized by the presence of a large N-terminal extracellular region. In addition, all aGPCRs but one (GPR123) contain a GPCR autoproteolysis-inducing (GAIN) domain that mediates autoproteolytic cleavage at the GPCR autoproteolysis site motif to generate N- and a C-terminal fragments (NTF and CTF, respectively) during protein maturation. Subsequently, the NTF and CTF are associated noncovalently as a heterodimer at the plasma membrane. While the biological function of the GAIN domain-mediated autocleavage is not fully understood, mounting evidence suggests that the NTF and CTF possess distinct biological activities in addition to their function as a receptor unit. We discuss recent advances in understanding the biological functions, signaling mechanisms, and disease associations of the aGPCRs.

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2014. Vol. 1333, 43-64 p.
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URN: urn:nbn:se:uu:diva-238747DOI: 10.1111/nyas.12580ISI: 000349698600003PubMedID: 25424900OAI: oai:DiVA.org:uu-238747DiVA: diva2:772058
Available from: 2014-12-16 Created: 2014-12-16 Last updated: 2015-03-30Bibliographically approved

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Schiöth, Helgi B
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