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Structural insights into brassinosteroid export mediated by the Arabidopsis ABC transporter ABCB1

Hong Wei, Heyuan Zhu (UGent) , Wei Ying, Hilde Janssens (UGent) , Miroslav Kvasnica, Johan M. Winne, Yongxiang Gao, Jiří Friml, Qian Ma (UGent) , Shutang Tan, et al.
(2025) PLANT COMMUNICATIONS. 6(1).
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Abstract
Brassinosteroids (BRs) are steroidal phytohormones indispensable for plant growth, development, and responses to environmental stresses. The export of bioactive BRs to the apoplast is essential for BR signalling initiation, which requires binding of BR molecule to the extracellular domains of the plasma membrane-localized receptor complex. We have previously shown that the Arabidopsis thaliana ATP-binding cassette (ABC) transporter, ABCB19, functions as a BR exporter, and together with its close homologue, ABCB1, positively regulate BR signalling. Here, we demonstrate that ABCB1 is another BR transporter. The ATP hydrolysis activity of ABCB1 was stimulated by bioactive BRs, and its transport activity was confirmed in proteoliposomes and protoplasts. Structures of ABCB1 in substrate-unbound (apo), brassinolide (BL)-bound, and ATP plus BL-bound states were determined. In the BL-bound structure, BL was bound to the hydrophobic cavity formed by the transmembrane domain, and triggered local conformational changes. Together, our data provide additional insights into the ABC transporter-mediated BR export.
Keywords
ABCB1, Arabidopsis, Brassinosteroid (BR), signalling, structure, transport, brassinosteroids, signaling, AUXIN TRANSPORT, EFFLUX, GENE, BIOSYNTHESIS, IMMUNOPHILIN, PERCEPTION, EXPRESSION, MECHANISM, THALIANA, PROTEINS

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MLA
Wei, Hong, et al. “Structural Insights into Brassinosteroid Export Mediated by the Arabidopsis ABC Transporter ABCB1.” PLANT COMMUNICATIONS, vol. 6, no. 1, 2025, doi:10.1016/j.xplc.2024.101181.
APA
Wei, H., Zhu, H., Ying, W., Janssens, H., Kvasnica, M., Winne, J. M., … Sun, L. (2025). Structural insights into brassinosteroid export mediated by the Arabidopsis ABC transporter ABCB1. PLANT COMMUNICATIONS, 6(1). https://doi.org/10.1016/j.xplc.2024.101181
Chicago author-date
Wei, Hong, Heyuan Zhu, Wei Ying, Hilde Janssens, Miroslav Kvasnica, Johan M. Winne, Yongxiang Gao, et al. 2025. “Structural Insights into Brassinosteroid Export Mediated by the Arabidopsis ABC Transporter ABCB1.” PLANT COMMUNICATIONS 6 (1). https://doi.org/10.1016/j.xplc.2024.101181.
Chicago author-date (all authors)
Wei, Hong, Heyuan Zhu, Wei Ying, Hilde Janssens, Miroslav Kvasnica, Johan M. Winne, Yongxiang Gao, Jiří Friml, Qian Ma, Shutang Tan, Xin Liu, Eugenia Russinova, and Linfeng Sun. 2025. “Structural Insights into Brassinosteroid Export Mediated by the Arabidopsis ABC Transporter ABCB1.” PLANT COMMUNICATIONS 6 (1). doi:10.1016/j.xplc.2024.101181.
Vancouver
1.
Wei H, Zhu H, Ying W, Janssens H, Kvasnica M, Winne JM, et al. Structural insights into brassinosteroid export mediated by the Arabidopsis ABC transporter ABCB1. PLANT COMMUNICATIONS. 2025;6(1).
IEEE
[1]
H. Wei et al., “Structural insights into brassinosteroid export mediated by the Arabidopsis ABC transporter ABCB1,” PLANT COMMUNICATIONS, vol. 6, no. 1, 2025.
@article{01JCFQGEAMYDFW5NCM7AKEGERJ,
  abstract     = {{Brassinosteroids (BRs) are steroidal phytohormones indispensable for plant growth, development, and responses to environmental stresses. The export of bioactive BRs to the apoplast is essential for BR signalling initiation, which requires binding of BR molecule to the extracellular domains of the plasma membrane-localized receptor complex. We have previously shown that the Arabidopsis thaliana ATP-binding cassette (ABC) transporter, ABCB19, functions as a BR exporter, and together with its close homologue, ABCB1, positively regulate BR signalling. Here, we demonstrate that ABCB1 is another BR transporter. The ATP hydrolysis activity of ABCB1 was stimulated by bioactive BRs, and its transport activity was confirmed in proteoliposomes and protoplasts. Structures of ABCB1 in substrate-unbound (apo), brassinolide (BL)-bound, and ATP plus BL-bound states were determined. In the BL-bound structure, BL was bound to the hydrophobic cavity formed by the transmembrane domain, and triggered local conformational changes. Together, our data provide additional insights into the ABC transporter-mediated BR export.}},
  articleno    = {{101181}},
  author       = {{Wei, Hong and Zhu, Heyuan and Ying, Wei and Janssens, Hilde and Kvasnica, Miroslav and Winne, Johan M. and Gao, Yongxiang and Friml, Jiří and Ma, Qian and Tan, Shutang and Liu, Xin and Russinova, Eugenia and Sun, Linfeng}},
  issn         = {{2590-3462}},
  journal      = {{PLANT COMMUNICATIONS}},
  keywords     = {{ABCB1,Arabidopsis,Brassinosteroid (BR),signalling,structure,transport,brassinosteroids,signaling,AUXIN TRANSPORT,EFFLUX,GENE,BIOSYNTHESIS,IMMUNOPHILIN,PERCEPTION,EXPRESSION,MECHANISM,THALIANA,PROTEINS}},
  language     = {{eng}},
  number       = {{1}},
  pages        = {{13}},
  title        = {{Structural insights into brassinosteroid export mediated by the Arabidopsis ABC transporter ABCB1}},
  url          = {{http://doi.org/10.1016/j.xplc.2024.101181}},
  volume       = {{6}},
  year         = {{2025}},
}
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