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Peer-reviewedCC BYNature Plants

A mechanistic framework for the recognition of chemically diverse brassinosteroids by BRI1-family receptor kinases

  • A. Caregnato1,2
  • Houming Chen1,2
  • Miroslav Kvasnica3,4
  • Ulrich Hohmann5,1,6,2
  • Jana Oklešťková3,4
  • Karoll Ferrer3,4
  • Larissa Broger1,2
  • Ludwig A. Hothorn7,8
  • Miroslav Strnad3,4
  • Michael Hothorn9,2
9 affiliations
  1. 1Structural Plant Biology Laboratory, Department of Plant Sciences, University of Geneva, Geneva, Switzerland
  2. 2Structural Plant Biology Laboratory, Department of Plant Science, University of Geneva, 2 Geneva, Switzerland
  3. 3Laboratory of Growth Regulators, Faculty of Science, Palacký University & Institute of Experimental Botany, The Czech Academy of Sciences, Olomouc, Czech Republic
  4. 4Laboratory of Growth Regulators, Faculty of Science, Palacky University & Institute of Experimental Botany, The Czech Academy of Sciences, CZ-77900, Olomouc, Czech Republic
  5. 5Institute of Molecular Biology, Mainz, Germany
  6. 6Institute of Molecular Biotechnology of the Austrian Academy of Sciences (IMBA) & Research Institute of Molecular Pathology (IMP), Vienna BioCenter (VBC), 100, Vienna, Austria
  7. 7Leibniz University Hannover, Hanover, Germany
  8. 8Retired from Leibniz University Hannover, Germany, present address: Im Grund 12, 31867 Lauenau, Germany
  9. 9Structural Plant Biology Laboratory, Department of Plant Sciences, University of Geneva, Geneva, Switzerland. [email protected]
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Abstract

Brassinosteroids (BRs) are chemically diverse plant steroid hormones produced via a branched biosynthetic pathway. The potent BR brassinolide is sensed by the membrane receptor kinase BRI1 and a SERK co-receptor, but the physiological functions of other abundant BRs remain to be characterized. Here we present quantitative binding kinetics for 4 Arabidopsis thaliana BR receptors and 15 BRs, which define the key chemical features required for high-affinity receptor binding, ligand positioning and co-receptor recognition. BRI1, BRL1 and BRL3 share overlapping ligand preferences, whereas BRL2 binds C 28 BRs with moderate affinity. Structural analyses of BR-bound BRI1 and BRL3 ectodomains combined with extensive in vitro and in vivo mutagenesis studies reveal a high structural plasticity of the hormone-binding pocket. Functional assays using structure-based BR agonists and antagonists uncover that BR receptor–co-receptor signalling complexes can recognize chemically diverse BRs, introducing an additional, intriguing layer of BR signalling regulation.

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Cite

BibTeXRIS
BibTeX
@article{caregnato2026mechanistic,
  title = {{A mechanistic framework for the recognition of chemically diverse brassinosteroids by BRI1-family receptor kinases}},
  author = {A. Caregnato and Houming Chen and Miroslav Kvasnica and Ulrich Hohmann and Jana Oklešťková and Karoll Ferrer and Larissa Broger and Ludwig A. Hothorn and Miroslav Strnad and Michael Hothorn},
  journal = {Nature Plants},
  year = {2026},
  month = aug,
  doi = {10.1038/s41477-026-02346-0},
  url = {https://doi.org/10.1038/s41477-026-02346-0},
  note = {CC BY},
}
RIS
TY  - JOUR
TI  - A mechanistic framework for the recognition of chemically diverse brassinosteroids by BRI1-family receptor kinases
AU  - A. Caregnato
AU  - Houming Chen
AU  - Miroslav Kvasnica
AU  - Ulrich Hohmann
AU  - Jana Oklešťková
AU  - Karoll Ferrer
AU  - Larissa Broger
AU  - Ludwig A. Hothorn
AU  - Miroslav Strnad
AU  - Michael Hothorn
PY  - 2026
DA  - 2026/08/05
JO  - Nature Plants
DO  - 10.1038/s41477-026-02346-0
UR  - https://doi.org/10.1038/s41477-026-02346-0
AB  - Brassinosteroids (BRs) are chemically diverse plant steroid hormones produced via a branched biosynthetic pathway. The potent BR brassinolide is sensed by the membrane receptor kinase BRI1 and a SERK co-receptor, but the physiological functions of other abundant BRs remain to be characterized. Here we present quantitative binding kinetics for 4 Arabidopsis thaliana BR receptors and 15 BRs, which define the key chemical features required for high-affinity receptor binding, ligand positioning and co-receptor recognition. BRI1, BRL1 and BRL3 share overlapping ligand preferences, whereas BRL2 binds C 28 BRs with moderate affinity. Structural analyses of BR-bound BRI1 and BRL3 ectodomains combined with extensive in vitro and in vivo mutagenesis studies reveal a high structural plasticity of the hormone-binding pocket. Functional assays using structure-based BR agonists and antagonists uncover that BR receptor–co-receptor signalling complexes can recognize chemically diverse BRs, introducing an additional, intriguing layer of BR signalling regulation.
SN  - 2055-026X
SN  - 2055-0278
ER  -