New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors.
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.
Liebscher, I; Ackley, B; Araç, D; Ariestanti, DM; Aust, G; Bae, B-I; Bista, BR; Bridges, JP; Duman, JG; Engel, FB; Giera, S; Goffinet, AM; Hall, RA; Hamann, J; Hartmann, N; Lin, H-H; Liu, M; Luo, R; Mogha, A; Monk, KR; Peeters, MC; Prömel, S; Ressl, S; Schiöth, HB; Sigoillot, SM; Song, H; Talbot, WS; Tall, GG; White, JP; Wolfrum, U; Xu, L; Piao, X
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