Molecular basis for redox control by the human cystine/glutamate antiporter system xc^.

ABSTRACT: Cysteine plays an essential role in cellular redox homoeostasis as a key constituent of the tripeptide glutathione (GSH). A rate limiting step in cellular GSH synthesis is the availability of cysteine. However, circulating cysteine exists in the blood as the oxidised di-peptide cystine, requiring specialised transport systems for its import into the cell. System xc^- is a dedicated cystine transporter, importing cystine in exchange for intracellular glutamate. To counteract elevated levels of reactive oxygen species in cancerous cells system xc^- is frequently upregulated, making it an attractive target for anticancer therapies. However, the molecular basis for ligand recognition remains elusive, hampering efforts to specifically target this transport system. Here we pr

SUBMITTER: Parker JL 

PROVIDER: S-EPMC8654953 | biostudies-literature | 2021 Dec

REPOSITORIES: biostudies-literature