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Ann N Y Acad Sci. 2014 Dec;1333:43-64. doi: 10.1111/nyas.12580. Epub 2014 Nov 25.

New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors.

Author information

1
Institute of Biochemistry, Molecular Biochemistry, Medical Faculty, University of Leipzig, Leipzig, Germany.

Abstract

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.

KEYWORDS:

adhesion G protein-coupled receptor; cancer; development; myelination; signal transduction; structural biology; synaptogenesis

PMID:
25424900
PMCID:
PMC4278406
DOI:
10.1111/nyas.12580
[Indexed for MEDLINE]
Free PMC Article

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