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.
Original language | English (US) |
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Pages (from-to) | 43-64 |
Number of pages | 22 |
Journal | Annals of the New York Academy of Sciences |
Volume | 1333 |
Issue number | 1 |
DOIs | |
State | Published - Dec 1 2014 |
Externally published | Yes |
Keywords
- Adhesion G protein-coupled receptor
- Cancer
- Development
- Myelination
- Signal transduction
- Structural biology
- Synaptogenesis
ASJC Scopus subject areas
- General Neuroscience
- General Biochemistry, Genetics and Molecular Biology
- History and Philosophy of Science