ArticleNature structural & molecular biology2025
Evolutionary analysis reveals the origin of sodium coupling in glutamate transporters.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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3 citing papers in PubMed.
- Structures of the sodium-coupled phosphate importer SLC34A2 reveal a distinct architecture and gating mechanism.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural and functional basis of proton-independent transition metal import by a canonical bacterial Nramp transporter.bioRxiv : the preprint server for biology · 2026Article
- Cryo-EM structures reveal the HLife science alliance · 2025Article
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Abstract
Secondary active membrane transporters harness the energy of ion gradients to concentrate their substrates. Homologous transporters evolved to couple transport to different ions in response to changing environments and needs. The bases of such diversification and, thus, principles of ion coupling are unexplored. Here, using phylogenetics and ancestral protein reconstruction, we investigated sodium-coupled transport in prokaryotic glutamate transporters, a mechanism ubiquitous across life domains and critical to neurotransmitter recycling in humans by excitatory amino acid transporters from the solute carrier 1 family. By inferring ancestral prokaryotic transporter sequences during a change in the ion-coupling mechanism, we found an evolutionary transition from sodium-dependent to independent substrate binding and transport. Structural and functional experiments on ancestral transporters suggest that the transition involved allosteric mutations, rendering sodium binding dispensable without affecting the ion-binding sites. Allosteric tuning of transporters' energy landscapes might be a widespread route of their functional diversification.
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