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New functions and signaling mechanisms for the class of adhesion G protein–coupled receptors
Author(s) -
Liebscher Ines,
Ackley Brian,
Araç Demet,
Ariestanti Donna M.,
Aust Gabriela,
Bae Byoungil,
Bista Bigyan R.,
Bridges James P.,
Duman Joseph G.,
Engel Felix B.,
Giera Stefanie,
Goffinet André M.,
Hall Randy A.,
Hamann Jörg,
Hartmann Nicole,
Lin HsiHsien,
Liu Mingyao,
Luo Rong,
Mogha Amit,
Monk Kelly R.,
Peeters Miriam C.,
Prömel Simone,
Ressl Susanne,
Schiöth Helgi B.,
Sigoillot Séverine M.,
Song Helen,
Talbot William S.,
Tall Gregory G.,
White James P.,
Wolfrum Uwe,
Xu Lei,
Piao Xianhua
Publication year - 2014
Publication title -
annals of the new york academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.712
H-Index - 248
eISSN - 1749-6632
pISSN - 0077-8923
DOI - 10.1111/nyas.12580
Subject(s) - receptor , microbiology and biotechnology , chemistry , signal transduction , adhesion , class (philosophy) , computational biology , biology , biochemistry , computer science , artificial intelligence , organic chemistry
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.