Structural insights into the substrate transport mechanism of the amino acid transporter complex.
Ontology highlight
ABSTRACT: The L-type amino acid transporter 1 (LAT1), in complex with its ancillary protein 4F2hc, mediates the sodium-independent antiport of large neutral amino acids across the plasma membrane. LAT1 preferentially transports substrates, such as L-leucine, L-tyrosine, and L-tryptophan, thyroid hormones, and drugs like 3,4-dihydroxyphenylalanine. Its pivotal role in cancer development and progression has established LAT1 as a promising therapeutic target. While prior studies have resolved the LAT1-4F2hc architecture and inhibitor interactions, the molecular basis of LAT1 substrate selectivity remains elusive. Here, we present the cryo-EM structures of LAT1-4F2hc bound to L-tyrosine, L-tryptophan, L-leucine, and 3,4-dihydro
SUBMITTER: Yang H
PROVIDER: S-EPMC12444478 | biostudies-literature | 2025 Aug
REPOSITORIES: biostudies-literature
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