ArticleNature communications2018
Structural characterisation reveals insights into substrate recognition by the glutamine transporter ASCT2/SLC1A5.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 86 citations in OpenAlex.
- LAT1-mediated amino acid metabolism reprogramming: a novel metabolic vulnerability in recurrent pituitary neuroendocrine tumors.Endocrine connections · 2026Article
- Preclinical Comparison ofJournal of nuclear medicine : official publication, Society of Nuclear Medicine · 2026Article
- The double-positive cells in the tumor microenvironment.Journal of translational internal medicine · 2026Article
- Evolutionary analysis reveals the origin of sodium coupling in glutamate transporters.Nature structural & molecular biology · 2025Article
- Itaconate transport across the plasma membrane and Salmonella-containing vacuole via MCT1/4 modulates macrophage antibacterial activity.Nature communications · 2025Article
- MRI of ASCT2-mediated amino acid uptake in xenograft tumor models.Research square · 2025Article
- Impacts of 360 mg/kg Niacinamide Supplementation in Low-Protein Diets on Energy and Nitrogen Metabolism and Intestinal Microbiota in Growing-Finishing Pigs.Animals : an open access journal from MDPI · 2025Article
- Targeting glutamine metabolism as a potential target for cancer treatment.Journal of experimental & clinical cancer research : CR · 2025Review
- Glutamine's double-edged sword: fueling tumor growth and offering therapeutic hope.Frontiers in immunology · 2025Review
- Epigenome-wide association study on the plasma metabolome suggests self-regulation of the glycine and serine pathway through DNA methylation.Clinical epigenetics · 2024Article
- Discovery and Synthesis of Hydroxy-l-Proline Blockers of the Neutral Amino Acid Transporters SLC1A4 (ASCT1) and SLC1A5 (ASCT2).Molecules (Basel, Switzerland) · 2024Article
- Glutamine Supplementation as an Anticancer Strategy: A Potential Therapeutic Alternative to the Convention.Cancers · 2024Review
- The Interaction between Collagen 1 and High Mannose Type CD133 Up-Regulates Glutamine Transporter SLC1A5 to Promote the Tumorigenesis of Glioblastoma Stem Cells.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024Article
- Characteristics of amino acid metabolism in colorectal cancer.World journal of clinical cases · 2023Review
- Targeting Glutamine Metabolism with a Novel Na+/K+-ATPase Inhibitor RX108 in Hepatocellular Carcinoma.Molecular cancer therapeutics · 2023Article
- A pan-cancer analysis of SLC1A5 in human cancers.Heliyon · 2023Article
- Targeting Glutamine Metabolism in Prostate Cancer.Frontiers in bioscience (Elite edition) · 2023Review
- Molecular insights into disease-associated glutamate transporter (EAAT1 /Frontiers in molecular biosciences · 2023Article
- Alanine serine cysteine transporter (ASCT) substrate binding site properties probed with hydroxyhomoserine esters.Journal of physical organic chemistry · 2022Article
- Characterizing unexpected interactions of a glutamine transporter inhibitor with members of the SLC1A transporter family.The Journal of biological chemistry · 2022Article
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Cancer cells undergo a shift in metabolism where they become reliant on nutrients such as the amino-acid glutamine. Glutamine enters the cell via the alanine/serine/cysteine transporter 2 (ASCT2) that is upregulated in several cancers to maintain an increased supply of this nutrient and are therefore an attractive target in cancer therapeutic development. ASCT2 belongs to the glutamate transporter (SLC1A) family but is the only transporter in this family able to transport glutamine. The structural basis for glutamine selectivity of ASCT2 is unknown. Here, we identify two amino-acid residues in the substrate-binding site that are responsible for conferring glutamine selectivity. We introduce corresponding mutations into a prokaryotic homologue of ASCT2 and solve four crystal structures, which reveal the structural basis for neutral amino acid and inhibitor binding in this family. This structural model of ASCT2 may provide a basis for future development of selective ASCT2 inhibitors to treat glutamine-dependent cancers.
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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.