Analysis of phosphorylation of the BRI1/BAK1 complex in arabidopsis reveals amino acid residues critical for receptor formation and activation of BR signaling.

@article{Yun2009AnalysisOP,
  title={Analysis of phosphorylation of the BRI1/BAK1 complex in arabidopsis reveals amino acid residues critical for receptor formation and activation of BR signaling.},
  author={Hye Sup Yun and Young Hee Bae and Yun Ji Lee and Soo Chang and Seong-Ki Kim and Jianming Li and Kyoung Hee Nam},
  journal={Molecules and cells},
  year={2009},
  volume={27 2},
  pages={183-90}
}
The plasma membrane-localized BRASSINOSTEROID-INSENSITIVE1 (BRI1) and BRI1-ASSOCIATED KINASE1 (BAK1) are a well-known receptor pair involved in brassinosteroids (BR) signaling in Arabidposis. The formation of a receptor complex in response to BRs and the subsequent activation of cytoplasmic domain kinase activity share mechanistic characteristics with animal receptor kinases. Here, we demonstrate that BRI1 and BAK1 are BR-dependently phosphorylated, and that phosphorylated forms of the two… CONTINUE READING

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