Liebscher I, Ackley B, Arac D, Ariestanti DM, Aust G, Bae BI, Bista BR, Bridges JP, Duman JG, Engel F, Giera S, Goffinet AM, Hall RA, Hamann J, Hartmann N, Lin HH, Liu M, Luo R, Mogha A, Monk KR, Peeters MC, Proemel S, Ressl S, Schioth HB, Sigoillot SM, Song H, Talbot WS, Tall GG, White JP, Wolfrum U, Xu L, Piao X (2014)
Publication Type: Journal article
Publication year: 2014
Book Volume: 1333
Pages Range: 43-64
Journal Issue: 1
DOI: 10.1111/nyas.12580
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 ?-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.
APA:
Liebscher, I., Ackley, B., Arac, D., Ariestanti, D.M., Aust, G., Bae, B.-I.,... Piao, X. (2014). New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors. Annals of the New York Academy of Sciences, 1333(1), 43-64. https://dx.doi.org/10.1111/nyas.12580
MLA:
Liebscher, Ines, et al. "New functions and signaling mechanisms for the class of adhesion G protein-coupled receptors." Annals of the New York Academy of Sciences 1333.1 (2014): 43-64.
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