| Literature DB >> 25424900 |
Ines Liebscher1, Brian Ackley, Demet Araç, Donna M Ariestanti, Gabriela Aust, Byoung-il Bae, Bigyan R Bista, James P Bridges, Joseph G Duman, Felix B Engel, Stefanie Giera, André M Goffinet, Randy A Hall, Jörg Hamann, Nicole Hartmann, Hsi-Hsien Lin, Mingyao Liu, Rong Luo, Amit Mogha, Kelly R Monk, Miriam C Peeters, Simone Prömel, Susanne Ressl, Helgi B Schiöth, Séverine M Sigoillot, Helen Song, William S Talbot, Gregory G Tall, James P White, Uwe Wolfrum, Lei Xu, Xianhua Piao.
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.Entities:
Keywords: adhesion G protein-coupled receptor; cancer; development; myelination; signal transduction; structural biology; synaptogenesis
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Year: 2014 PMID： 25424900 PMCID： PMC4278406 DOI： 10.1111/nyas.12580
Source DB: PubMed Journal: Ann N Y Acad Sci ISSN： 0077-8923 Impact factor: 5.691