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.
journal_name
Ann N Y Acad Scijournal_title
Annals of the New York Academy of Sciencesauthors
Liebscher I,Ackley B,Araç D,Ariestanti DM,Aust G,Bae BI,Bista BR,Bridges JP,Duman JG,Engel FB,Giera S,Goffinet AM,Hall RA,Hamann J,Hartmann N,Lin HH,Liu M,Luo R,Mogha A,Monk KR,Peeters MC,Prömel S,Ressl S,Scdoi
10.1111/nyas.12580subject
Has Abstractpub_date
2014-12-01 00:00:00pages
43-64eissn
0077-8923issn
1749-6632journal_volume
1333pub_type
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