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Science 25 July 2008:
Vol. 321. no. 5888, pp. 557 - 560
DOI: 10.1126/science.1156973
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Reports

BSKs Mediate Signal Transduction from the Receptor Kinase BRI1 in Arabidopsis

Wenqiang Tang,1 Tae-Wuk Kim,1 Juan A. Oses-Prieto,2 Yu Sun,1 Zhiping Deng,1 Shengwei Zhu,1,3 Ruiju Wang,1,4 Alma L. Burlingame,2 Zhi-Yong Wang1*

Brassinosteroids (BRs) bind to the extracellular domain of the receptor kinase BRI1 to activate a signal transduction cascade that regulates nuclear gene expression and plant development. Many components of the BR signaling pathway have been identified and studied in detail. However, the substrate of BRI1 kinase that transduces the signal to downstream components remains unknown. Proteomic studies of plasma membrane proteins lead to the identification of three homologous BR-signaling kinases (BSK1, BSK2, and BSK3). The BSKs are phosphorylated by BRI1 in vitro and interact with BRI1 in vivo. Genetic and transgenic studies demonstrate that the BSKs represent a small family of kinases that activate BR signaling downstream of BRI1. These results demonstrate that BSKs are the substrates of BRI1 kinase that activate downstream BR signal transduction.

1 Department of Plant Biology, Carnegie Institution of Washington, Stanford, CA 94305, USA.
2 Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143, USA.
3 Key Laboratory of Photosynthesis and Environmental Molecular Biology, Institute of Botany, Chinese Academy of Sciences, Beijing 100093, China.
4 Institute for Molecular Biology, College of Life Science, Nankai University, Tianjin 300071, China.

* To whom correspondence should be addressed. E-mail: zywang24{at}stanford.edu

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THIS ARTICLE HAS BEEN CITED BY OTHER ARTICLES:
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H. Guo, L. Li, H. Ye, X. Yu, A. Algreen, and Y. Yin (2009)
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Function of the {alpha} Subunit of Rice Heterotrimeric G Protein in Brassinosteroid Signaling.
K. Oki, N. Inaba, K. Kitagawa, S. Fujioka, H. Kitano, Y. Fujisawa, H. Kato, and Y. Iwasaki (2009)
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Science. ISSN 0036-8075 (print), 1095-9203 (online)