Identification of a stereotypic molecular arrangement of endogenous glycine receptors at spinal cord synapses.

ABSTRACT: Precise quantitative information about the molecular architecture of synapses is essential to understanding the functional specificity and downstream signaling processes at specific populations of synapses. Glycine receptors (GlyRs) are the primary fast inhibitory neurotransmitter receptors in the spinal cord and brainstem. These inhibitory glycinergic networks crucially regulate motor and sensory processes. Thus far, the nanoscale organization of GlyRs underlying the different network specificities has not been defined. Here, we have quantitatively characterized the molecular arrangement and ultra-structure of glycinergic synapses in spinal cord tissue using quantitative super-resolution correlative light and electron microscopy. We show that endogenous GlyRs exhibit equal receptor-scaffo

SUBMITTER: Maynard SA 

PROVIDER: S-EPMC8752092 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature