ArticleThe EMBO journal1999
Amino acid transport of y+L-type by heterodimers of 4F2hc/CD98 and members of the glycoprotein-associated amino acid transporter family.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.
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Who cites it
68 citing papers in PubMed, 270 citations in OpenAlex.
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- Structural basis for the substrate recognition and transport mechanism of the human yScience advances · 2025Article
- Mechanisms involved in aminoacidurias: impacts of genetic and environmental factors.Current research in physiology · 2025Review
- Prognostic and immunotherapeutic potential of disulfidptosis-associated signature in pancreatic cancer.Frontiers in immunology · 2025Article
- Low crude protein formulation with supplemental amino acids for its impacts on intestinal health and growth performance of growing-finishing pigs.Journal of animal science and biotechnology · 2024Article
- The human LAT1-4F2hc (SLC7A5-SLC3A2) transporter complex: Physiological and pathophysiological implications.Basic & clinical pharmacology & toxicology · 2023Review
- Do Amino Acid Antiporters Have Asymmetric Substrate Specificity?Biomolecules · 2023Article
- Amino Acid Homeostasis in Mammalian Cells with a Focus on Amino Acid Transport.The Journal of nutrition · 2022Article
- Heteromeric Amino Acid Transporters in Brain: from Physiology to Pathology.Neurochemical research · 2022Review
- Analysis of L-leucine amino acid transporter species activity and gene expression by human blood brain barrier hCMEC/D3 model reveal potential LAT1, LAT4, BJournal of cerebral blood flow and metabolism : official journal of the International Society of Cerebral Blood Flow and Metabolism · 2022Article
- Factors Influencing Proteolysis and Protein Utilization in the Intestine of Pigs: A Review.Animals : an open access journal from MDPI · 2021Review
- Article
- Expression of proposed methionine transporters along the gastrointestinal tract of pigs and their regulation by dietary methionine sources.Genes & nutrition · 2021Article
- The Adipose Tissue-Derived Secretome (ADS) in Obesity Uniquely Induces L-Type Amino Acid Transporter 1 (LAT1) and mTOR Signaling in Estrogen-Receptor-Positive Breast Cancer Cells.International journal of molecular sciences · 2021Article
- Analysis of Host Jejunum Transcriptome and Associated Microbial Community Structure Variation in Young Calves with Feed-Induced Acidosis.Metabolites · 2021Article
- Oncogenic transformation of NIH/3T3 cells by the overexpression of L-type amino acid transporter 1, a promising anti-cancer target.Oncotarget · 2021Article
- Immunotherapy using IgE or CAR T cells for cancers expressing the tumor antigen SLC3A2.Journal for immunotherapy of cancer · 2021Article
- Biphasic regulation of glutamine consumption by WNT during osteoblast differentiation.Journal of cell science · 2021Article
- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
8 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Amino acid transport across cellular membranes is mediated by multiple transporters with overlapping specificities. We recently have identified the vertebrate proteins which mediate Na+-independent exchange of large neutral amino acids corresponding to transport system L. This transporter consists of a novel amino acid permease-related protein (LAT1 or AmAT-L-lc) which for surface expression and function requires formation of disulfide-linked heterodimers with the glycosylated heavy chain of the h4F2/CD98 surface antigen. We show that h4F2hc also associates with other mammalian light chains, e.g. y+LAT1 from mouse and human which are approximately 48% identical with LAT1 and thus belong to the same family of glycoprotein-associated amino acid transporters. The novel heterodimers form exchangers which mediate the cellular efflux of cationic amino acids and the Na+-dependent uptake of large neutral amino acids. These transport characteristics and kinetic and pharmacological fingerprints identify them as y+L-type transport systems. The mRNA encoding my+LAT1 is detectable in most adult tissues and expressed at high levels in kidney cortex and intestine. This suggests that the y+LAT1-4F2hc heterodimer, besides participating in amino acid uptake/secretion in many cell types, is the basolateral amino acid exchanger involved in transepithelial reabsorption of cationic amino acids; hence, its defect might be the cause of the human genetic disease lysinuric protein intolerance.
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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.