The CDG1 Kinase Mediates Brassinosteroid Signal Transduction from BRI1 Receptor Kinase to BSU1 Phosphatase and GSK3-like Kinase BIN2

被引:332
作者
Kim, Tae-Wuk [1 ]
Guan, Shenheng [2 ]
Burlingame, Alma L. [2 ]
Wang, Zhi-Yong [1 ]
机构
[1] Carnegie Inst Washington, Dept Plant Biol, Stanford, CA 94305 USA
[2] Univ Calif San Francisco, Dept Pharmaceut Chem, San Francisco, CA 94143 USA
关键词
TRANSCRIPTION FACTORS; GENE-EXPRESSION; PLANT-GROWTH; TYROSINE PHOSPHORYLATION; ARABIDOPSIS-THALIANA; PLASMA-MEMBRANE; PROTEIN-KINASE; BZR1; ELONGATION; BRI1/BAK1;
D O I
10.1016/j.molcel.2011.05.037
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The brassinosteroid (BR) signaling Pathway includes two receptor-like kinases (BRI1 and BAK1), a plasma membrane-associated kinase (BSK1), two phosphatases (BSU1 and PP2A), a GSK3-like kinase (BIN2), and two homologous transcription factors (BZR1 and BES1/BZR2). But the mechanisms of signal relay are not fully understood. Here, we show that a receptor-like cytoplasmic kinase named CDG1 mediates signal transduction from BRI1 to BSU1. Transgenic experiments confirm that CDG1 and its homolog CDL1 positively regulate BR signaling and plant growth. Mass spectrometry analysis identified BRI1 phosphorylation sites in CDG1 and CDG1 phosphorylation sites in BSU1. Mutations of these phosphorylation sites compromised the BR signaling functions. The results demonstrate that BRI1 phosphorylates S234 to activate CDG1 kinase, and CDG1 in turn phosphorylates S764 to activate BSU1, which inactivates BIN2 by dephosphorylating Y200 of BIN2. This study thus demonstrates a complete phosphorylation/dephosphorylation cascade linking a steroid-activated receptor kinase to a GSK3-like kinase in plants.
引用
收藏
页码:561 / 571
页数:11
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