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TitleStructural basis for pH-responsive amino acid transport via SLC7A4.
Journal, issue, pagesNat Commun, Year 2026
Publish dateMar 28, 2026
AuthorsDimitrios Kolokouris / Anuja Bothra / Takafumi Kato / Yi C Zeng / Simon Lichtinger / Joanne L Parker / Philip C Biggin / Simon Newstead /
PubMed AbstractThe transport of amino acids across cell membranes is essential for metabolism, neuronal signalling, and immune system function. The amino acid polyamine organocation (APC) superfamily controls amino ...The transport of amino acids across cell membranes is essential for metabolism, neuronal signalling, and immune system function. The amino acid polyamine organocation (APC) superfamily controls amino acid transport via mechanisms including amino acid exchange, facilitative diffusion, and sodium- or proton-coupled transport. Although many mammalian APC members functioning as exchangers and sodium-coupled systems have been identified, the mechanisms underlying pH-regulated amino acid transport in mammalian cells remain unclear. Here, we show that the plasma membrane amino acid transporter SLC7A4 is regulated by low extracellular pH and functions as a leucine transporter in human cells. Using Cryo-EM structures of the plant homologue, CAT4, from Arabidopsis thaliana in outward-open apo and L-ornithine-bound states, as well as transport assays and molecular dynamics simulations based on homology models of the human transporter, we identify residues responsible for amino acid selectivity that supports an allosteric mechanism linking ligand recognition to pH regulation. This mechanism is consistent with an evolutionary link to proton-coupled prokaryotic homologues. Overall, our findings provide a structural and functional basis for pH-gated leucine transport by the human SLC7A4 transporter and provides a framework for understanding amino acid selectivity within the wider SLC7 family.
External linksNat Commun / PubMed:41904136
MethodsEM (single particle)
Resolution4.23 Å
Structure data

55110

9sqh

EMDB-55110, PDB-9sqh:
Cryo-EM structure of the Arabidopsis thaliana CAT4 transporter in the outward-open apo state (without synthetic nanobody)
Method: EM (single particle) / Resolution: 4.23 Å

Source
  • arabidopsis thaliana (thale cress)
KeywordsTRANSPORT PROTEIN / cationic amino acid transporter / APC fold / LeuT fold / cholesterol / outward-open state / cationic amino acids / SLC7 / MEMBRANE PROTEIN

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