Homodimerization of a proximal region within the C-terminus of the orphan G-protein coupled receptor GPR179. (October 2021)

• Record Type: Journal Article
• Authors: Bachert, Wolfrat; Klotz, Lisa; Sticht, Heinrich; Enz, Ralf
• Is Part Of: Neurochemistry international. Volume 149(2021)
• Publication Date: 2021-10
• Subjects: GPR179 -- mGluR6 -- C-terminus -- Protein-protein interaction -- Coiled-coil -- Retina; CT C-terminus -- GABA γ-amino butyric acid -- GPCR G-protein coupled receptor -- mGluR metabotropic glutamate receptor -- RGS regulator of G-protein signalling -- R9AP RGS anchor protein 9 -- TRPM1 transient receptor potential cation channel subfamily member 1; Neurochemistry -- Periodicals; Neurochemistry -- Periodicals; Neurochimie -- Périodiques; Neurochemistry; Periodicals; 612.804205
• DOI: 10.1016/j.neuint.2021.105150
• Languages: English
• ISSNs: 0197-0186

Abstract

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.