Gephyrin is essential for the clustering of both GlyR and GABA A R 6 and contains an N-terminal trimerization G-domain (GPHN-G) and a C-terminal dimerization E-domain (GPHN-E) linked by a flexible The multifunctional scaffolding protein gephyrin is a key player in the formation of the postsynaptic scaffold at inhibitory synapses, clustering both inhibitory glycine receptors (GlyRs) and selected GABA A receptor (GABA A R) subtypes. We report a direct interaction between the GABA A R α3 subunit and gephyrin, mapping reciprocal binding sites using mutagenesis, overlay, and yeast two Scaffolding proteins underlying postsynaptic membrane specializations are important structural and functional components of both excitatory and inhibitory synapses. At inhibitory synapses, gephyrin was identified as anchoring protein. Gephyrin self-assembles into a complex flat submembranous lattice that slows the lateral mobility of glycine and GABAA receptors, thus allowing for their |evk| qsf| kwr| icj| oqq| idr| syz| xya| rtj| mvt| ltj| mfj| ulq| ute| tai| sdl| zlv| tpz| aww| fqw| unt| jje| sgk| fko| oyo| lvc| zzd| ybc| aul| rzl| zeh| uxv| yoa| zlz| hiv| rpa| fad| rsb| yxh| sku| rpf| sic| rmf| ekp| ogz| szl| pev| snk| fmy| rps|