Cited by 846Plant Molecular Biology ResearchPlant biochemistry and biosynthesisPlant Reproductive Biology

BRI1 is a critical component of a plasma-membrane receptor for plant steroids

Wang, Zhi-Yong, Seto, Hideharu, Fujioka, Shozo, Yoshida, Shigeo, Chory, Joanne·2001·Nature

Abstract

Most multicellular organisms use steroids as signalling molecules for physiological and developmental regulation. Two different modes of steroid action have been described in animal systems: the well-studied gene regulation response mediated by nuclear receptors, and the rapid non-genomic responses mediated by proposed membrane-bound receptors. Plant genomes do not seem to encode members of the nuclear receptor superfamily. However, a transmembrane receptor kinase, brassinosteroid-insensitive1 (BRI1), has been implicated in brassinosteroid responses. Here we show that BRI1 functions as a receptor of brassinolide, the most active brassinosteroid. The number of brassinolide-binding sites and the degree of response to brassinolide depend on the level of BRI1 protein. The brassinolide-binding activity co-immunoprecipitates with BRI1, and requires a functional BRI1 extracellular domain. Moreover, treatment of Arabidopsis seedlings with brassinolide induces autophosphorylation of BRI1, which, together with our binding studies, shows that BRI1 is a receptor kinase that transduces steroid signals across the plasma membrane.

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Crossref · 10.1038/35066597

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25 of 25 references verified0 citation errors · 0 not checkable

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  • Animal steroid hormones act through the nuclear receptor family of transcription factors, while plant brassinosteroids signal through a cell surface receptor kinase-mediated signal transduction pathway.

    “While animal steroid hormones act through nuclear receptor family of transcription factors, plant brassinosteroids signal through a cell surface receptor kinase-mediated signal transduction pathway (8, 9).”

    From Anabolic effect of plant brassinosteroid (2011) · cites this paper as [8]

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Authors
Wang, Z.-Y., Seto, H., Fujioka, S., Yoshida, S., & Chory, J.
Affiliations
  • RIKEN (JP)
  • Salk Institute for Biological Studies (US)
Corresponding author
Chory, Joanne
Venue
Nature
Published
2001-03-15
Volume
410
Issue
6826
Pages
380-383
ISSN
  • 0028-0836 (ISSN-L)
  • 1476-4687
OpenAlex
W1994207647
Cited by
846
References
25
Citations by year
2026: 17 · 2025: 31 · 2024: 33 · 2023: 32 · 2022: 40 · 2021: 30 · 2020: 30 · 2019: 25 · 2018: 30 · 2017: 44 · 2016: 29 · 2015: 26 · 2014: 27 · 2013: 40 · 2012: 26
FWCI
66.86
Type
journal article
Language
en
Open access
closed
Locations
  • Nature (publishedVersion)
  • PubMed (publishedVersion)
  • RePEc: Research Papers in Economics (submittedVersion)
Funders
  • National Science Foundation
  • Howard Hughes Medical Institute
  • U.S. Department of Agriculture
  • National Alliance for Research on Schizophrenia and Depression
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant biochemistry and biosynthesis
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Plant Reproductive Biology
Keywords
BRI1, brassinosteroid signaling, brassinolide, plasma membrane receptors, receptor kinases, autophosphorylation, Arabidopsis thaliana
MeSH terms
Cholestanols, Enzyme Activation, Ligands, Mutation, Phosphorylation, Phytosterols, Protein Kinases, Receptors, Steroid, Steroids, Heterocyclic, Signal Transduction, Genes, Plant, Arabidopsis, Protein Structure, Tertiary, Arabidopsis Proteins, Brassinosteroids

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