Reciprocal stabilization of glycine receptors and gephyrin scaffold proteins at inhibitory synapses.

ABSTRACT: Postsynaptic scaffold proteins immobilize neurotransmitter receptors in the synaptic membrane opposite to presynaptic vesicle release sites, thus ensuring efficient synaptic transmission. At inhibitory synapses in the spinal cord, the main scaffold protein gephyrin assembles in dense molecule clusters that provide binding sites for glycine receptors (GlyRs). Gephyrin and GlyRs can also interact outside of synapses, where they form receptor-scaffold complexes. Although several models for the formation of postsynaptic scaffold domains in the presence of receptor-scaffold interactions have been advanced, a clear picture of the coupled dynamics of receptors and scaffold proteins at synapses is lacking. To characterize the GlyR and gephyrin dynamics at inhibitory synapses, we performed fluoresc

SUBMITTER: Chapdelaine T 

PROVIDER: S-EPMC8008324 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature