Target intelligence / Profile preview

b(0,+)-type amino acid transporter 1 (b(0,+)AT1)

Target
b(0,+)AT1
Molecular classification
Transporter (solute carrier family), Heteromeric amino acid transporter (HAT), Antiporter (electrogenic exchanger), Amino acid/polyamine/organocation (APC) superfamily member
01

Overview

System b0,+ amino acid transporter (b(0,+)-type amino acid transporter 1; SLC7A9) is a heteromeric membrane transporter comprising a polytopic light chain (SLC7A9) and a single-transmembrane heavy chain partner (typically rBAT/SLC3A1). It mediates sodium-independent, electrogenic exchange between cationic amino acids (such as lysine and arginine), neutral amino acids, and cystine mainly in the brush border of renal and intestinal epithelial cells. The transporter is essential for reabsorption of filtered cystine and dibasic amino acids from the urine; mutations lead to cystinuria, a hereditary disorder characterized by kidney stones. Its structure includes a LeuT fold and alternating access mechanism for substrate binding and translocation. In cancer, the transporter may be upregulated to support increased amino acid demand and is considered a potential therapeutic target. System b0,+ is distinct from other SLC family amino acid transporters in substrate specificity, structure, and physiological role.

Other names
SLC7A9b(0,+)ATBAT1System b(0,+)b(0,+) amino acid transporterdibasic and neutral amino acid transporterAssociated complex: rBAT (SLC3A1)
02

Mechanism of action

Competitive inhibition of amino acid transport (blocking substrate recognition or translocation); Interference with antiporter exchange cycles; Alteration of cell amino acid pools and viability in disease or cancer context.

03

Biological functions

Amino acid transmembrane transport (cationic and neutral amino acids)L-cystine transmembrane transportElectrogenic exchange (in kidney and intestine brush border)Maintenance of amino acid pools (homeostasis)Regulation of nitrogen metabolism
04

Disease associations

Cystinuria (type I and non-type I)—loss-of-function mutations cause cystinuria due to defective cystine and arginine reabsorption in the kidneyCancer (upregulated in some tumors to support arginine demand and growth)Potential involvement in other metabolic diseases
05

Safety considerations

Risk of amino acid imbalance if inhibited systemically (possible metabolic toxicity)Genetic deficiency leads to cystinuria—stone formation due to cystine precipitationAssociated protein trafficking defects (e.g., ER retention when mutants)
06

Interacting drugs

Methyl-DL-tryptophan (α-MT)

2 more in the full profile.

07

Biomarkers

Mutations in SLC7A9 (e.g., T216M, Gly105Arg, Glu mutations) for cystinuria diagnosis and carrier statusExpression level (potentially upregulated in certain cancers as a metabolic biomarker)Associated urinary amino acid patterns (cystinuria)

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