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Volume 24, No 11, Nov 2014

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 24 Issue 11, November 2014: 1328-1341

ORIGINAL ARTICLES

Structural insights into the negative regulation of BRI1 signaling by BRI1-interacting protein BKI1

Jie Wang1,*, Jianjun Jiang2,*, Jue Wang1,*, Lei Chen1, Shi-Long Fan1, Jia-Wei Wu1, Xuelu Wang2,3 and Zhi-Xin Wang1

1MOE Key Laboratory for Protein Science, School of Life Sciences, Tsinghua University, Beijing 100084, China
2State Key Laboratory of Genetic Engineering and Institute of Plant Biology, School of Life Sciences, Fudan University, Shanghai 200433, China
3College of Life Science and Technology, Huazhong Agricultural University, Wuhan, Hubei 430070, China
Correspondence: Zhi-Xin Wang,(zhixinwang@mail.tsinghua.edu.cn)

Brassinosteroids (BRs) are essential steroid hormones that have crucial roles in plant growth and development. BRs are perceived by the cell-surface receptor-like kinase brassinosteroid insensitive 1 (BRI1). In the absence of BRs, the cytosolic kinase domain (KD) of BRI1 is inhibited by its auto-inhibitory carboxyl terminus, as well as by interacting with an inhibitor protein, BRI1 kinase inhibitor 1 (BKI1). How BR binding to the extracellular domain of BRI1 leads to activation of the KD and dissociation of BKI1 into the cytosol remains unclear. Here we report the crystal structure of BRI1 KD in complex with the interacting peptide derived from BKI1. We also provide biochemical evidence that BRI1-associated kinase 1 (BAK1) plays an essential role in initiating BR signaling. Steroid-dependent heterodimerization of BRI1 and BAK1 ectodomains brings their cytoplasmic KDs in the right orientation for competing with BKI1 and transphosphorylation.


10.1038/cr.2014.132

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