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Letters to Nature
Nature 410, 380-383 (15 March 2001) | doi:10.1038/35066597; Received 3 October 2000; Accepted 20 December 2000
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BRI1 is a critical component of a plasma-membrane receptor for plant steroids
Zhi-Yong Wang1, Hideharu Seto2, Shozo Fujioka2, Shigeo Yoshida2 & Joanne Chory1
- Howard Hughes Medical Institute and Plant Biology Laboratory, The Salk Institute for Biological Studies, 10010 N. Torrey Pines Road, La Jolla, California 92037, USA
- Plant Functions Lab, RIKEN (The Institute of Physical and Chemical Research), Wako-shi, Saitama 351-0198, Japan
Correspondence to: Joanne Chory1 Correspondence and requests for materials should be addressed to J.C. (e-mail: Email: chory@salk.edu).
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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