GABABR is composed of two subunits, namely GABABR1 and GABABR2, which should heterodimerize to form the fully functional receptor. Up to date, seven splice variants of GABABR1 and three splice variants of GABABR2 have been found. The tissue distribution of these splice variants in CNS is reviewed. It has shown that the extracellular domain of GABABR1 but not GABABR2 is responsible for the ligand binding. The carbon terminal of GABABR1 exists the intracellular retention signal, which results in the failure of expression of GABABR1 in the cell surface. Upon the heterologous expression of GABABR2, the GABABR1 can be trafficked to the cell surface properly, and the ligand binding efficiency increases. GABABR2 plays an important role in the couple of receptor with G-protein. The function of the subdomains of GABABR1 and GABABR2 is discussed. GABABR can interact with transcription factor directly.
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