ArticleNature plants2023
Cryo-EM structure and molecular mechanism of abscisic acid transporter ABCG25.
Article in Nature plants, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed, 28 citations in OpenAlex.
- Beyond membrane transport: Transporters as dynamic signal integrators for plant signaling and adaptation.Plant communications · 2026Review
- Apoplast Engineering Unveiled: Multi-Target Strategies to Disarm Pathogens and Elevate Global Food Security.Plant, cell & environment · 2026Review
- Abscisic Acid-Mediated Drought Tolerance inCurrent issues in molecular biology · 2026Review
- Regulation of apocarotenoids for quality improvement and biofortification of horticultural crops.Journal of advanced research · 2026Review
- Article
- Conformational cycle and small-molecule inhibition mechanism of a plant ABCB transporter in lipid membranes.Science advances · 2025Article
- A key residue of the extracellular gate provides quality control contributing to ABCG substrate specificity.Nature communications · 2025Article
- Message hidden in α-helices-toward a better understanding of plant ABCG transporters' multispecificity.Plant physiology · 2025Article
- ABA importers ABCG17 and ABCG18 redundantly regulate seed size in Arabidopsis.The Plant journal : for cell and molecular biology · 2025Article
- Structural insights into brassinosteroid export mediated by the Arabidopsis ABC transporter ABCB1.Plant communications · 2025Article
- Cryo-EM structure and molecular mechanism of the jasmonic acid transporter ABCG16.Nature plants · 2024Article
- Inhibition and transport mechanisms of the ABC transporter hMRP5.Nature communications · 2024Article
- Structural insights into AtABCG25, an angiosperm-specific abscisic acid exporter.Plant communications · 2024Article
- Unveiling the crucial roles of abscisic acid in plant physiology: implications for enhancing stress tolerance and productivity.Frontiers in plant science · 2024Review
Corrections and comments
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Authors and funding
10 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Abscisic acid (ABA) is one of the plant hormones that regulate various physiological processes, including stomatal closure, seed germination and development. ABA is synthesized mainly in vascular tissues and transported to distal sites to exert its physiological functions. Many ABA transporters have been identified, however, the molecular mechanism of ABA transport remains elusive. Here we report the cryogenic electron microscopy structure of the Arabidopsis thaliana adenosine triphosphate-binding cassette G subfamily ABA exporter ABCG25 (AtABCG25) in inward-facing apo conformation, ABA-bound pre-translocation conformation and outward-facing occluded conformation. Structural and biochemical analyses reveal that the ABA bound with ABCG25 adopts a similar configuration as that in ABA receptors and that the ABA-specific binding is dictated by residues from transmembrane helices TM1, TM2 and TM5a of each protomer at the transmembrane domain interface. Comparison of different conformational structures reveals conformational changes, especially those of transmembrane helices and residues constituting the substrate translocation pathway during the cross-membrane transport process. Based on the structural data, a 'gate-flipper' translocation model of ABCG25-mediated ABA cross-membrane transport is proposed. Our structural data on AtABCG25 provide new clues to the physiological study of ABA and shed light on its potential applications in plants and agriculture.
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