ArticleProceedings of the National Academy of Sciences of the United States of America2014
Structural bases for the interaction and stabilization of the human amino acid transporter LAT2 with its ancillary protein 4F2hc.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.
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52 citing papers in PubMed, 86 citations in OpenAlex.
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- Structural basis for the substrate recognition and transport mechanism of the human yScience advances · 2025Article
- Cryo-EM structure of the human Asc-1 transporter complex.Nature communications · 2024Article
- Over-Production of the Human SLC7A10 inInternational journal of molecular sciences · 2023Article
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- ER-localized Shr3 is a selective co-translational folding chaperone necessary for amino acid permease biogenesis.The Journal of cell biology · 2023Article
- Abnormal triaging of misfolded proteins by adult neuronal ceroid lipofuscinosis-associated DNAJC5/CSPα mutants causes lipofuscin accumulation.Autophagy · 2023Article
- CD98 heavy chain as a prognostic biomarker and target for cancer treatment.Frontiers in oncology · 2023Review
- Growth, Cannibalism, and 5-TH Metabolism in Pufferfish (Aquaculture nutrition · 2023Article
- Characterization of substrates and inhibitors of the human heterodimeric transporter 4F2hc-LAT1 using purified protein and the scintillation proximity radioligand binding assay.Frontiers in physiology · 2023Article
- Describing inhibitor specificity for the amino acid transporter LAT1 from metainference simulations.Biophysical journal · 2022Article
- Structure of the human heterodimeric transporter 4F2hc-LAT2 in complex with Anticalin, an alternative binding protein for applications in single-particle cryo-EM.Scientific reports · 2022Article
- N-glycosylation is crucial for trafficking and stability of SLC3A2 (CD98).Scientific reports · 2022Article
- Integrated AlphaFold2 and DEER investigation of the conformational dynamics of a pH-dependent APC antiporter.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural investigation of human cystine/glutamate antiporter system xFrontiers in molecular biosciences · 2022Article
- Heteromeric Amino Acid Transporters in Brain: from Physiology to Pathology.Neurochemical research · 2022Review
- 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
- Identification by proximity labeling of novel lipidic and proteinaceous potential partners of the dopamine transporter.Cellular and molecular life sciences : CMLS · 2021Article
- The Ectodomains of rBAT and 4F2hc Are Fake or Orphan α-Glucosidases.Molecules (Basel, Switzerland) · 2021Review
- Rush Hour of LATs towards Their Transport Cycle.Membranes · 2021Review
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Authors and funding
9 authors at 6 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Heteromeric amino acid transporters (HATs) are the unique example, known in all kingdoms of life, of solute transporters composed of two subunits linked by a conserved disulfide bridge. In metazoans, the heavy subunit is responsible for the trafficking of the heterodimer to the plasma membrane, and the light subunit is the transporter. HATs are involved in human pathologies such as amino acidurias, tumor growth and invasion, viral infection and cocaine addiction. However structural information about interactions between the heavy and light subunits of HATs is scarce. In this work, transmission electron microscopy and single-particle analysis of purified human 4F2hc/L-type amino acid transporter 2 (LAT2) heterodimers overexpressed in the yeast Pichia pastoris, together with docking analysis and crosslinking experiments, reveal that the extracellular domain of 4F2hc interacts with LAT2, almost completely covering the extracellular face of the transporter. 4F2hc increases the stability of the light subunit LAT2 in detergent-solubilized Pichia membranes, allowing functional reconstitution of the heterodimer into proteoliposomes. Moreover, the extracellular domain of 4F2hc suffices to stabilize solubilized LAT2. The interaction of 4F2hc with LAT2 gives insights into the structural bases for light subunit recognition and the stabilizing role of the ancillary protein in HATs.
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