Issue Information

Front cover:Background: The C-terminal domain (CTD) of mGluR6 (residues 840-871) interacts with PDZ (postsynaptic density 95/discs large/zonula occludens-1)-containing scaffold proteins and G βγ subunits. We investigated whether CTD contributes to mGluR6 cell surface localization and receptor function. Immunocytochemical, biochemical, and electrophysiological approaches showed that deletions in the distal half of CTD attenuated mGluR6 surface localization and G-protein coupling, while further deletions comprising the distal two-thirds restored these functions. A sequence analysis revealed a putative ER retention motif, arginine-(Xaa)-arginine, in the middle of mGluR6 CTD, which was conserved among group III mGluRs. These results suggest that CTD is required for mGluR6 cell surfac e transportation and receptor function, while it may contain regulatory elements for intracellular trafficking and signaling.Image content: Triple immunofluorescence image of the subcellular localization of Δ858-871 mGluR6 mutant in transfected 293T cells. Surface localization (green) and total cellular expression (magenta) were assessed using DAPI counterstaining (cyan).Read the full article ‘Involvement of the C-terminal domain in cell surface localization and G-protein coupling of mGluR6’ by D. Rai, T. Akagi, A. Shimohata, T. Ishii, M. Gangi, T. Maruyama, Y. Wada-Kiyama, I. Ogiwara and M. Kaneda (J. Neurochem. 2021, vol. 158 (4), pp. 837 –848) on doi:10.1111/jnc.15217
Source: Journal of Neurochemistry - Category: Neuroscience Tags: Issue Information Source Type: research