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

Zhi-Yong Wang, Hideharu Seto, Shozo Fujioka, Shigeo Yoshida and Joanne Chory ()
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Zhi-Yong Wang: Howard Hughes Medical Institute and Plant Biology Laboratory, The Salk Institute for Biological Studies
Hideharu Seto: Plant Functions Lab, RIKEN (The Institute of Physical and Chemical Research)
Shozo Fujioka: Plant Functions Lab, RIKEN (The Institute of Physical and Chemical Research)
Shigeo Yoshida: Plant Functions Lab, RIKEN (The Institute of Physical and Chemical Research)
Joanne Chory: Howard Hughes Medical Institute and Plant Biology Laboratory, The Salk Institute for Biological Studies

Nature, 2001, vol. 410, issue 6826, 380-383

Abstract: 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.

Date: 2001
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DOI: 10.1038/35066597

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