Alpha subunit-dependent glycine receptor clustering and regulation of synaptic receptor numbers.

ABSTRACT: Accumulation of glycine receptors at synapses requires the interaction between the beta subunit of the receptor and the scaffold protein gephyrin. Here, we questioned whether different alpha subunits could modulate the receptors' diffusion and propensity to cluster at spinal cord synapses. Using quantitative photoactivated localisation microscopy we found that alpha-1 and alpha-3 containing glycine receptors display the same α₃:β₂ stoichiometry and gephyrin binding. Despite these similarities, alpha-3 containing receptors are less mobile and cluster at higher density compared to alpha-1, with 1500 versus 1100 complexes µm^-2, respectively. Furthermore, we identified a subunit-specific regulation of glycine receptor copy numbers at synapses: when challenged w

SUBMITTER: Patrizio A 

PROVIDER: S-EPMC5589798 | biostudies-literature | 2017 Sep

REPOSITORIES: biostudies-literature