ArticleProceedings of the National Academy of Sciences of the United States of America2016
Structure of Bor1 supports an elevator transport mechanism for SLC4 anion exchangers.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed.
- Structural and dynamic insights into SPDT for phosphorus allocation in rice.Science China. Life sciences · 2026Article
- Transport mechanism of the SLC4 proteins-Lessons from recent structural and computational studies.The Journal of biological chemistry · 2026Review
- Cryo-EM structures and transport mechanism of human multifunctional transporter BTR1.Protein & cell · 2026Article
- Convergent evolution increases boron transport through SNPs and tandem duplications atProceedings of the National Academy of Sciences of the United States of America · 2026Article
- Impact of anionic lipids on the energy landscape of conformational transition in anion exchanger 1 (AE1).Nature communications · 2025Article
- Genome-wide identification of boron transporters (GhBORs) in upland cotton and the role of GhBOR1 in promoting flowering.BMC plant biology · 2025Article
- Inactivation mechanisms of NaCommunications biology · 2025Article
- Molecular determinants of [Formula: see text] and cation transport in the human cation-dependent ClAmerican journal of physiology. Cell physiology · 2025Article
- The Bor1 elevator transport cycle is subject to autoinhibition and activation.Nature communications · 2024Article
- Interdomain-linkers control conformational transitions in the SLC23 elevator transporter UraA.Nature communications · 2024Article
- Molecular dynamics simulations of lipid-protein interactions in SLC4 proteins.Biophysical journal · 2024Article
- Mechanism of anion exchange and small-molecule inhibition of pendrin.Nature communications · 2024Article
- Structures and mechanisms of the Arabidopsis cytokinin transporter AZG1.Nature plants · 2024Article
- Elevator-like movements of prestin mediate outer hair cell electromotility.Nature communications · 2023Article
- Structural insights into the conformational changes of BTR1/SLC4A11 in complex with PIPNature communications · 2023Article
- Substrate binding and inhibition of the anion exchanger 1 transporter.Nature structural & molecular biology · 2023Article
- Structural basis of vitamin C recognition and transport by mammalian SVCT1 transporter.Nature communications · 2023Article
- Borate Transporters and SLC4 Bicarbonate Transporters Share Key Functional Properties.Membranes · 2023Article
- CryoEM structures of anion exchanger 1 capture multiple states of inward- and outward-facing conformations.Communications biology · 2022Article
- Transmembrane helices 5 and 12 control transport dynamics, substrate affinity, and specificity in the elevator-type UapA transporter.Genetics · 2022Article
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2 authors.
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Abstract
Boron is essential for plant growth because of its incorporation into plant cell walls; however, in excess it is toxic to plants. Boron transport and homeostasis in plants is regulated in part by the borate efflux transporter Bor1, a member of the solute carrier (SLC) 4 transporter family with homology to the human bicarbonate transporter Band 3. Here, we present the 4.1-Å resolution crystal structure of Arabidopsis thaliana Bor1. The structure displays a dimeric architecture in which dimerization is mediated by centralized Gate domains. Comparisons with a structure of Band 3 in an outward-open state reveal that the Core domains of Bor1 have rotated inwards to achieve an occluded state. Further structural comparisons with UapA, a xanthine transporter from the nucleobase-ascorbate transporter family, show that the downward pivoting of the Core domains relative to the Gate domains may access an inward-open state. These results suggest that the SLC4, SLC26, and nucleobase-ascorbate transporter families all share an elevator transport mechanism in which alternating access is provided by Core domains that carry substrates across a membrane.
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