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G-protein coupled receptors (GPCRs) play an essential role in eukaryotic cells signaling. According to phylogenetic analysis, most GPCRs belong to one of four classes, i.e. A, B, C, and Frizzled (Lagerstrom and Schioth, 2008). The class-C GPCR family contains metabotropic glutamate receptors (mGluR), γ-aminobutyric acid B receptors (GABAB receptor or GBR), several taste-sensing receptors (e.g. TAS1), and a Ca2+-sensing receptor (CaS). One characteristic feature of the class-C GPCRs is their dimerization, either into homo- or hetero-dimers, which is obligatory for function (Kniazeff et al., 2011). Each subunit in the dimer usually consists of an amino (N)-terminal extracellular domain (ECD) which binds orthosteric agonists, a linker peptide, a 7-transmembrane (TM) domain, and a cytosolic tail of varying lengths at the carboxyl (C)-terminus. It is well-established that all domains spare the linker peptide participating in the dimerization process (Rondard et al., 2008; Huang et al., 2011; Rondard et al., 2006). Further, it is believed that, after transmission of the ligand-binding signal from the ECD region to the 7-TM domain, the activation of the class-C GPCR dimer is associated with a conformational change of the 7-TM domain on the cytosol side, enabling binding and activation of downstream G-proteins. In contrast, the precise details of the mechanisms for signal transduction from the ligand binding site in the ECD region to the cytosolic side of the 7-TM domain, where downstream G-proteins are activated, remain to be elucidated.

Why is dimerization essential for class-C GPCR function? New insights from mGluR1 crystal structure analysis