Homodimerization of a proximal region within the C-terminus of the orphan G-protein coupled receptor GPR179

Abstract

G-protein coupled receptors exhibit numerous biological functions. The orphan G-protein coupled receptor GPR179 is a central component of a 1 Megadalton large signalling complex in the ON-pathway of the mammalian retina that assembles multiple proteins, including the metabotropic glutamate receptor mGluR6. Dimer formation is a hallmark of G-protein coupled receptors and some use intracellular C-termini for dimerization. Here we tested the dimerization properties of the intracellular C-terminal domains of mGluR6 and GPR179. While the C-termini of GPR179 and mGluR6 did not interact, we detected a robust homodimerization of a proximal region in the GPR179 C-terminus. Mapping studies defined a linear stretch of 64 amino acids as dimerization region. Bioinformatic analysis indicated that this dimerization region might adopt an α-helical structure that is predicted to dimerize by forming a coiled-coil. Based on these data, we speculate that homodimerization of GPR179 might contribute to the formation of large signalling complexes in the mammalian retina.