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RESEARCH PRODUCT

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

Gabriela AustBrian D. AckleyJoseph G. DumanJörg HamannAndré M. GoffinetStefanie GieraBigyan R. BistaByoung-il BaeMingyao LiuUwe WolfrumRong LuoLei XuHelgi B. SchiöthRandy A. HallSusanne ResslAmit MoghaDemet AraçHsi-hsien LinSéverine M. SigoillotJames P. WhiteMiriam C. PeetersHelen SongFelix B. EngelJames P. BridgesGregory G. TallInes LiebscherXianhua PiaoDonna Maretta AriestantiNicole HartmannWilliam S. TalbotKelly R. MonkSimone Prömel

subject

History and Philosophy of ScienceStructural biologyGeneral NeuroscienceExtracellularSignal transductionBiologyCell adhesionReceptorProtein maturationGeneral Biochemistry Genetics and Molecular BiologyFunction (biology)G protein-coupled receptorCell biology

description

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.

yearjournalcountryeditionlanguage
2014-11-25Annals of the New York Academy of Sciences
https://doi.org/10.1111/nyas.12580