ArticleThe Journal of biological chemistry2009
A conserved Na(+) binding site of the sodium-coupled neutral amino acid transporter 2 (SNAT2).
Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
17 citing papers in PubMed, 34 citations in OpenAlex.
- Surface Avidity of Anionic Polypeptide Coatings on Layer-by-Layer Nanoparticles Target Cancer-Associated Amino Acid Transporters.Angewandte Chemie (International ed. in English) · 2026Article
- Exploring Amino Acid Transporters as Therapeutic Targets for Cancer: An Examination of Inhibitor Structures, Selectivity Issues, and Discovery Approaches.Pharmaceutics · 2024Review
- Sodium-Dependent Neutral Amino Acid Transporter 2 Can Serve as a Tertiary Carrier for l-Type Amino Acid Transporter 1-Utilizing Prodrugs.Molecular pharmaceutics · 2023Article
- Yeast Plasma Membrane Fungal Oligopeptide Transporters Display Distinct Substrate Preferences despite Their High Sequence Identity.Journal of fungi (Basel, Switzerland) · 2021Article
- Rush Hour of LATs towards Their Transport Cycle.Membranes · 2021Review
- AhABI4s Negatively Regulate Salt-Stress Response in Peanut.Frontiers in plant science · 2021Article
- Metabolic Control over mTOR-Dependent Diapause-like State.Developmental cell · 2020Article
- Regulation of Amino Acid Transport in Saccharomyces cerevisiae.Microbiology and molecular biology reviews : MMBR · 2019Review
- Crystal structure of arginine-bound lysosomal transporter SLC38A9 in the cytosol-open state.Nature structural & molecular biology · 2018Article
- Effects of Sodium and Amino Acid Substrate Availability upon the Expression and Stability of the SNAT2 (SLC38A2) Amino Acid Transporter.Frontiers in pharmacology · 2018Article
- Na+ coordination at the Na2 site of the Na+/I- symporter.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Identification of a Disulfide Bridge in Sodium-Coupled Neutral Amino Acid Transporter 2(SNAT2) by Chemical Modification.PloS one · 2016Article
- Membrane transporters for the special amino acid glutamine: structure/function relationships and relevance to human health.Frontiers in chemistry · 2014Review
- Membrane topological structure of neutral system N/A amino acid transporter 4 (SNAT4) protein.The Journal of biological chemistry · 2011Article
- The C-terminal domain of the neutral amino acid transporter SNAT2 regulates transport activity through voltage-dependent processes.The Biochemical journal · 2011Article
- Conformational rearrangements to the intracellular open states of the LeuT and ApcT transporters are modulated by common mechanisms.Biophysical journal · 2010Article
- Structural perspectives on secondary active transporters.Trends in pharmacological sciences · 2010Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
The SLC38 family of solute transporters mediates the coupled transport of amino acids and Na(+) into or out of cells. The structural basis for this coupled transport process is not known. Here, a profile-based sequence analysis approach was used, predicting a distant relationship with the SLC5/6 transporter families. Homology models using the LeuT(Aa) and Mhp1 transporters of known structure as templates were established, predicting the location of a conserved Na(+) binding site in the center of membrane helices 1 and 8. This homology model was tested experimentally in the SLC38 member SNAT2 by analyzing the effect of a mutation to Thr-384, which is predicted to be part of this Na(+) binding site. The results show that the T384A mutation not only inhibits the anion leak current, which requires Na(+) binding to SNAT2, but also dramatically lowers the Na(+) affinity of the transporter. This result is consistent with a previous analysis of the N82A mutant transporter, which has a similar effect on anion leak current and Na(+) binding and which is also expected to form part of the Na(+) binding site. In contrast, random mutations to other sites in the transporter had little or no effect on Na(+) affinity. Our results are consistent with a cation binding site formed by transmembrane helices 1 and 8 that is conserved among the SLC38 transporters as well as among many other bacterial and plant transporter families of unknown structure, which are homologous to SLC38.
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Registered trials
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.