ArticleProceedings of the National Academy of Sciences of the United States of America2013
Functional identification and characterization of sodium binding sites in Na symporters.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.
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Who cites it
29 citing papers in PubMed, 38 citations in OpenAlex.
- Glucose transporters and sodium glucose co-transporters cooperatively import glucose into energy-demanding organs in carcinogenic liver fluke Clonorchis sinensis.PLoS neglected tropical diseases · 2024Article
- Membrane potential accelerates sugar uptake by stabilizing the outward facing conformation of the Na/glucose symporter vSGLT.Nature communications · 2023Article
- Functional characterization of SGLT1 using SSM-based electrophysiology: Kinetics of sugar binding and translocation.Frontiers in physiology · 2023Article
- Article
- Rush Hour of LATs towards Their Transport Cycle.Membranes · 2021Review
- Function Trumps Form in Two Sugar Symporters,International journal of molecular sciences · 2021Review
- Active Glucose Transport 2020 and Beyond.Function (Oxford, England) · 2021Article
- A comprehensive overview of substrate specificity of glycoside hydrolases and transporters in the small intestine : "A gut feeling".Cellular and molecular life sciences : CMLS · 2020Review
- Mapping of Ion and Substrate Binding Sites in Human Sodium Iodide Symporter (hNIS).Journal of chemical information and modeling · 2020Article
- Locking Two Rigid-body Bundles in an Outward-Facing Conformation: The Ion-coupling Mechanism in a LeuT-fold Transporter.Scientific reports · 2019Article
- L amino acid transporter structure and molecular bases for the asymmetry of substrate interaction.Nature communications · 2019Article
- The molecular mechanism of SLC34 proteins: insights from two decades of transport assays and structure-function studies.Pflugers Archiv : European journal of physiology · 2019Review
- Inhibitor binding mode and allosteric regulation of NaNature communications · 2018Article
- Intestinal Saturated Long-Chain Fatty Acid, Glucose and Fructose Transporters and Their Inhibition by Natural Plant Extracts in Caco-2 Cells.Molecules (Basel, Switzerland) · 2018Review
- Physiology of renal glucose handling via SGLT1, SGLT2 and GLUT2.Diabetologia · 2018Review
- Conformational transitions of the sodium-dependent sugar transporter, vSGLT.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Active site voltage clamp fluorometry of the sodium glucose cotransporter hSGLT1.Proceedings of the National Academy of Sciences of the United States of America · 2017Article
- Novel and Unexpected Functions of SGLTs.Physiology (Bethesda, Md.) · 2017Review
- The Sodium/Iodide Symporter (NIS): Molecular Physiology and Preclinical and Clinical Applications.Annual review of physiology · 2017Review
- Structural and functional significance of water permeation through cotransporters.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
Sodium cotransporters from several different gene families belong to the leucine transporter (LeuT) structural family. Although the identification of Na(+) in binding sites is beyond the resolution of the structures, two Na(+) binding sites (Na1 and Na2) have been proposed in LeuT. Na2 is conserved in the LeuT family but Na1 is not. A biophysical method has been used to measure sodium dissociation constants (Kd) of wild-type and mutant human sodium glucose cotransport (hSGLT1) proteins to identify the Na(+) binding sites in hSGLT1. The Na1 site is formed by residues in the sugar binding pocket, and their mutation influences sodium binding to Na1 but not to Na2. For the canonical Na2 site formed by two -OH side chains, S392 and S393, and three backbone carbonyls, mutation of S392 to cysteine increased the sodium Kd by sixfold. This was accompanied by a dramatic reduction in the apparent sugar and phlorizin affinities. We suggest that mutation of S392 in the Na2 site produces a structural rearrangement of the sugar binding pocket to disrupt both the binding of the second Na(+) and the binding of sugar. In contrast, the S393 mutations produce no significant changes in sodium, sugar, and phlorizin affinities. We conclude that the Na2 site is conserved in hSGLT1, the side chain of S392 and the backbone carbonyl of S393 are important in the first Na(+) binding, and that Na(+) binding to Na2 promotes binding to Na1 and also sugar binding.
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