ArticleScientific reports2020
ATP modulates SLC7A5 (LAT1) synergistically with cholesterol.
Article in Scientific reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 30 citations in OpenAlex.
- Structural basis of anticancer drug recognition and amino acid transport by LAT1.Nature communications · 2025Article
- The conserved lysine residue in transmembrane helix 5 is pivotal for the cytoplasmic gating of the L-amino acid transporters.PNAS nexus · 2025Article
- Comprehensive Characterization of LAT1 Cholesterol-Binding Sites.Journal of chemical theory and computation · 2024Article
- Over-Production of the Human SLC7A10 inInternational journal of molecular sciences · 2023Article
- LAT1 (SLC7A5) catalyzes copper(histidinate) transport switching from antiport to uniport mechanism.iScience · 2023Article
- Insights into the Transport Cycle of LAT1 and Interaction with the Inhibitor JPH203.International journal of molecular sciences · 2023Article
- TMBIM5 is the CaEMBO reports · 2022Article
- Describing inhibitor specificity for the amino acid transporter LAT1 from metainference simulations.Biophysical journal · 2022Article
- Structural and functional investigation of ABC transporter STE6-2p fromProceedings of the National Academy of Sciences of the United States of America · 2022Article
- Bacterial over-expression of functionally active human CT2 (SLC22A16) carnitine transporter.Molecular biology reports · 2022Article
- Strategies for Successful Over-Expression of Human Membrane Transport Systems Using Bacterial Hosts: Future Perspectives.International journal of molecular sciences · 2022Review
- Production of recombinant human xCT (SLC7A11) and reconstitution in proteoliposomes for functional studies.Frontiers in physiology · 2022Article
- Effective prediction of potential ferroptosis critical genes in clinical colorectal cancer.Frontiers in oncology · 2022Article
- The Nutraceutical Alliin From Garlic Is a Novel Substrate of the Essential Amino Acid Transporter LAT1 (SLC7A5).Frontiers in pharmacology · 2022Article
- Structural basis for substrate specificity of heteromeric transporters of neutral amino acids.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Chemical Approaches for Studying the Biology and Pharmacology of Membrane Transporters: The Histidine/Large Amino Acid Transporter SLC7A5 as a Benchmark.Molecules (Basel, Switzerland) · 2021Review
- Article
- Review
- Amino Acid Transporter LAT1 (SLC7A5) Mediates MeHg-Induced Oxidative Stress Defense in the Human Placental Cell Line HTR-8/SVneo.International journal of molecular sciences · 2021Article
- Yeast Cell-Based Transport Assay for the Functional Characterization of Human 4F2hc-LAT1 and -LAT2, and LAT1 and LAT2 Substrates and Inhibitors.Frontiers in molecular biosciences · 2021Article
Corrections and comments
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Authors and funding
9 authors at 3 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The plasma membrane transporter hLAT1 is responsible for providing cells with essential amino acids. hLAT1 is over-expressed in virtually all human cancers making the protein a hot-spot in the fields of cancer and pharmacology research. However, regulatory aspects of hLAT1 biology are still poorly understood. A remarkable stimulation of transport activity was observed in the presence of physiological levels of cholesterol together with a selective increase of the affinity for the substrate on the internal site, suggesting a stabilization of the inward open conformation of hLAT1. A synergistic effect by ATP was also observed only in the presence of cholesterol. The same phenomenon was detected with the native protein. Altogether, the biochemical assays suggested that cholesterol and ATP binding sites are close to each other. The computational analysis identified two neighboring regions, one hydrophobic and one hydrophilic, to which cholesterol and ATP were docked, respectively. The computational data predicted interaction of the ϒ-phosphate of ATP with Lys 204, which was confirmed by site-directed mutagenesis. The hLAT1-K204Q mutant showed an impaired function and response to ATP. Interestingly, this residue is conserved in several members of the SLC7 family.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.