ArticleThe Biochemical journal2001
Association of 4F2hc with light chains LAT1, LAT2 or y+LAT2 requires different domains.
Article in The Biochemical journal, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.
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Who cites it
26 citing papers in PubMed, 48 citations in OpenAlex.
- SLC3A2 promotes early-stage of Zika virus infection in human placental cells and astrocytes.Infectious diseases & immunity · 2026Article
- CD98hc controls CNS angiogenesis and blood-brain barrier integrity through localized regulation of the systemic integrin-FAK pathway.Nature cardiovascular research · 2026Article
- Interlaboratory Variability in the Madin-Darby Canine Kidney Cell Proteome.Molecular pharmaceutics · 2023Article
- Do Amino Acid Antiporters Have Asymmetric Substrate Specificity?Biomolecules · 2023Article
- Effect of Chronic Cadmium Exposure on Brain and Liver Transporters and Drug-Metabolizing Enzymes in Male and Female Mice Genetically Predisposed to Alzheimer's Disease.Drug metabolism and disposition: the biological fate of chemicals · 2022Article
- The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases.Molecules (Basel, Switzerland) · 2021Review
- The zebrafish cationic amino acid transporter/glycoprotein-associated family: sequence and spatiotemporal distribution during development of the transport system bFish physiology and biochemistry · 2021Article
- A GC-MS/Single-Cell Method to Evaluate Membrane Transporter Substrate Specificity and Signaling.Frontiers in molecular biosciences · 2021Article
- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
- Methyl-Metabolite Depletion Elicits Adaptive Responses to Support Heterochromatin Stability and Epigenetic Persistence.Molecular cell · 2020Article
- Wnt regulates amino acid transporter Slc7a5 and so constrains the integrated stress response in mouse embryos.EMBO reports · 2020Article
- Cryo-EM structure of the human L-type amino acid transporter 1 in complex with glycoprotein CD98hc.Nature structural & molecular biology · 2019Article
- Altered Expression of Small Intestinal Drug Transporters and Hepatic Metabolic Enzymes in a Mouse Model of Familial Alzheimer's Disease.Molecular pharmaceutics · 2018Article
- Blood-brain barrier transport machineries and targeted therapy of brain diseases.BioImpacts : BI · 2016Review
- Involvement of the L-Type Amino Acid Transporter Lat2 in the Transport of 3,3'-Diiodothyronine across the Plasma Membrane.European thyroid journal · 2015Article
- Novel cystine ester mimics for the treatment of cystinuria-induced urolithiasis in a knockout mouse model.Urology · 2014Article
- Structural bases for the interaction and stabilization of the human amino acid transporter LAT2 with its ancillary protein 4F2hc.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
- Membrane transporters for the special amino acid glutamine: structure/function relationships and relevance to human health.Frontiers in chemistry · 2014Review
- Homeostatic and innate immune responses: role of the transmembrane glycoprotein CD98.Cellular and molecular life sciences : CMLS · 2012Review
- The lipid raft-associated protein CD98 is required for vaccinia virus endocytosis.Journal of virology · 2012Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heterodimeric amino acid transporters are comprised of a type-II membrane protein named the heavy chain (4F2hc or rBAT) that may associate with a number of different polytopic membrane proteins, called light chains. It is thought that the heavy chain is mainly involved in the trafficking of the complex to the plasma membrane, whereas the transport process itself is catalysed by the light chain. The 4F2 heavy chain (4F2hc) associates with at least six different light chains to induce distinct amino acid-transport activites. To test if the light chains are specifically recognized and to identify domains involved in the recognition of light chains, C-terminally truncated mutants of 4F2hc were constructed and co-expressed with the light chains LAT1, LAT2 and y(+)LAT2. The truncated isoform T1, comprised of only 133 amino acids that form the cytosolic N-terminus and the transmembrane helix, displayed only a slight reduction in its ability to promote LAT1 expression at the membrane surface compared with the 529 amino acid wild-type 4F2hc protein. Co-expression of increasingly larger 4F2hc mutants caused a delayed translocation of LAT1. In contrast to the weak effects of 4F2hc truncations on LAT1 expression, surface expression of LAT2 and y(+)LAT2 was almost completely lost with all truncated heavy chains. Co-expression of LAT1 together with the other light chains did not result in displacement of LAT2 and y(+)LAT2. The results suggest that extracellular domains of the heavy chain are responsible mainly for recognition of light chains other than LAT1 and that the extracellular domain ensures proper translocation to the plasma membrane.
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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.