Cationic amino acid transporter 1 (SLC7A1) (CAT-1)

Cationic amino acid transporter 1 (CAT-1), encoded by the SLC7A1 gene, is a high-affinity, low-capacity permease responsible for the sodium-independent transport of basic amino acids such as L-arginine, L-lysine, and L-histidine [1, 2]. Beyond its physiological role in maintaining cellular amino acid homeostasis and providing substrates for nitric oxide synthesis, CAT-1 serves as the primary cellular receptor for ecotropic murine leukemia viruses (MuLV) [3, 4]. Other related MuLV entry receptors include the phosphate transporters PiT-1 (SLC20A1) and PiT-2 (SLC20A2), which facilitate the entry of gibbon ape leukemia virus and amphotropic MuLV, respectively, as well as XPR1 for xenotropic and polytropic MuLV [4]. This dual functionality of CAT-1 makes it a critical component in both metabolic regulation and viral pathogenesis. In clinical contexts, CAT-1 is often exploited as a gateway for gene therapy vectors derived from MuLV, and its overexpression has been linked to increased proliferation in various cancers, including colorectal and breast malignancies [5]. Furthermore, its role in arginine transport is vital for endothelial function, where it supports the production of nitric oxide, a key regulator of vascular tone [1]. Consequently, CAT-1 and its related receptors represent significant targets for understanding viral entry mechanisms and developing strategies for metabolic or oncological interventions.

Other names

Solute carrier family 7 member 1SLC7A1ATRC1ERRREC1LEcotropic retrovirus receptorSystem y+ basic amino acid transporterCAT1

Facilitates the transport of cationic amino acids (arginine, lysine, histidine) across the plasma membrane via a sodium-independent, pH-insensitive mechanism (System y+). It also acts as a high-affinity receptor for the envelope glycoprotein of ecotropic murine leukemia viruses, mediating viral attachment and subsequent membrane fusion.