Cross-Linking and Functional Analyses for Dimerization of a Cysteine Mutant of Glycine Transporter 1.

ABSTRACT: Glycine transporter 1 (GlyT1) is responsible for the reuptake of glycine, which regulates glutamate signaling as a co-agonist with N-methyl-D-aspartic acid (NMDA) receptors in the excitatory synapse and has been proposed to be a potential target in the development of therapies for a broad range of disorders of the central nervous system. Despite significant progress in characterizing structure and transport mechanism of the transporter, the regulation of transport function through oligomerization remains to be understood. In the present work, association of two forms of GlyT1 into dimers and higher order oligomers was detected by coimmunoprecipitation. To investigate functional properties of dimers of a GlyT1 cysteine mutant L288C, we performed oxidative cross-linking of the positioned cys

SUBMITTER: Wang J 

PROVIDER: S-EPMC9781295 | biostudies-literature | 2022 Dec

REPOSITORIES: biostudies-literature