ArticlePloS one2014
Detergent-induced stabilization and improved 3D map of the human heteromeric amino acid transporter 4F2hc-LAT2.
Article in PloS one, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.
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19 citing papers in PubMed, 30 citations in OpenAlex.
- Structural basis for the substrate recognition and transport mechanism of the human yScience advances · 2025Article
- Cell-Free Systems and Their Importance in the Study of Membrane Proteins.The Journal of membrane biology · 2025Review
- Cryo-EM structure of the human Asc-1 transporter complex.Nature communications · 2024Article
- 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
- 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
- Article
- Review
- 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
- Heteromeric Solute Carriers: Function, Structure, Pathology and Pharmacology.Advances in experimental medicine and biology · 2021Review
- The Heavy Chain 4F2hc Modulates the Substrate Affinity and Specificity of the Light Chains LAT1 and LAT2.International journal of molecular sciences · 2020Article
- Sub-Nanometer Cryo-EM Density Map of the Human Heterodimeric Amino Acid Transporter 4F2hc-LAT2.International journal of molecular sciences · 2020Article
- Subdomain cryo-EM structure of nodaviral replication protein A crown complex provides mechanistic insights into RNA genome replication.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Cryo-EM structure of the human heteromeric amino acid transporter bScience advances · 2020Article
- Article
- Volta Phase Plate Cryo-EM Structure of the Human Heterodimeric Amino Acid Transporter 4F2hc-LAT2.International journal of molecular sciences · 2019Article
- Regulatory Aspects of the Vacuolar CAT2 Arginine Transporter ofInternational journal of molecular sciences · 2019Article
- Modulation of LAT1 (SLC7A5) transporter activity and stability by membrane cholesterol.Scientific reports · 2017Article
- Structural insights into thyroid hormone transport mechanisms of the L-type amino acid transporter 2.Molecular endocrinology (Baltimore, Md.) · 2015Article
- End-product diacylglycerol enhances the activity of PI-PLC through changes in membrane domain structure.Biophysical journal · 2015Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human heteromeric amino acid transporters (HATs) are membrane protein complexes that facilitate the transport of specific amino acids across cell membranes. Loss of function or overexpression of these transporters is implicated in several human diseases such as renal aminoacidurias and cancer. HATs are composed of two subunits, a heavy and a light subunit, that are covalently connected by a disulphide bridge. Light subunits catalyse amino acid transport and consist of twelve transmembrane α-helix domains. Heavy subunits are type II membrane N-glycoproteins with a large extracellular domain and are involved in the trafficking of the complex to the plasma membrane. Structural information on HATs is scarce because of the difficulty in heterologous overexpression. Recently, we had a major breakthrough with the overexpression of a recombinant HAT, 4F2hc-LAT2, in the methylotrophic yeast Pichia pastoris. Microgram amounts of purified protein made possible the reconstruction of the first 3D map of a human HAT by negative-stain transmission electron microscopy. Here we report the important stabilization of purified human 4F2hc-LAT2 using a combination of two detergents, i.e., n-dodecyl-β-D-maltopyranoside and lauryl maltose neopentyl glycol, and cholesteryl hemisuccinate. The superior quality and stability of purified 4F2hc-LAT2 allowed the measurement of substrate binding by scintillation proximity assay. In addition, an improved 3D map of this HAT could be obtained. The detergent-induced stabilization of the purified human 4F2hc-LAT2 complex presented here paves the way towards its crystallization and structure determination at high-resolution, and thus the elucidation of the working mechanism of this important protein complex at the molecular level.
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