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 receptors1,2, and the rapid non-genomic responses mediated by proposed membrane-bound receptors3,4. Plant genomes do not seem to encode members of the nuclear receptor superfamily5. However, a transmembrane receptor kinase, brassinosteroid-insensitive1 (BRI1), has been implicated in brassinosteroid responses6,7. 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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Acknowledgements
We thank M. Chen for comments and L. Barden for technical assistance on the manuscript; D. Vafeados for technical assistance; and D. Friedrichsen for providing the BRI1–GFP line. This work was supported by a grant from the USDA and the Howard Hughes Medical Institute to J.C., and by a Grant-in-Aid for Scientific Research from the Ministry of Education, Science, Sports, and Culture of Japan to S.F.. Z.W. is an NSF postdoctoral fellow and J.C. is an Associate Investigator of the Howard Hughes Medical Institute.
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Wang, ZY., Seto, H., Fujioka, S. et al. BRI1 is a critical component of a plasma-membrane receptor for plant steroids. Nature 410, 380–383 (2001). https://doi.org/10.1038/35066597
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DOI: https://doi.org/10.1038/35066597