Chloride-dependent conformational changes in the GlyT1 glycine transporter.

ABSTRACT: The human GlyT1 glycine transporter requires chloride for its function. However, the mechanism by which Cl^- exerts its influence is unknown. To examine the role that Cl^- plays in the transport cycle, we measured the effect of Cl^- on both glycine binding and conformational changes. The ability of glycine to displace the high-affinity radioligand [³H]CHIBA-3007 required Na⁺ and was potentiated over 1,000-fold by Cl^- We generated GlyT1b mutants containing reactive cysteine residues in either the extracellular or cytoplasmic permeation pathways and measured changes in the reactivity of those cysteine residues as indicators of conformational changes in response to ions and substrate. Na⁺ increased accessibility in the

SUBMITTER: Zhang YW 

PROVIDER: S-EPMC7958241 | biostudies-literature | 2021 Mar

REPOSITORIES: biostudies-literature