Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1-Reference-Cited by-同舟云学术

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Structural basis for the impact of phosphorylation on the activation of plant receptor-like kinase BAK1

Published:2012-05-01 Issue:8 Volume:22 Page:1304-1308
ISSN:1001-0602
Container-title:Cell Research
language:en
Short-container-title:Cell Res

Author:

Yan Liming,Ma Yuanyuan,Liu Dan,Wei Xiaochao,Sun Yuna,Chen Xiaoyue,Zhao Huadong,Zhou Jingwen,Wang Zhiyong,Shui Wenqing,Lou Zhiyong

Publisher

Springer Science and Business Media LLC

Subject

Cell Biology,Molecular Biology

Link

http://www.nature.com/articles/cr201274.pdf

Reference15 articles.

1. Tang W, Deng Z, Wang ZY . Proteomics shed light on the brassinosteroid signaling mechanisms. Curr Opin Plant Biol 2011; 13:27–33.

2. Li J, Wen J, Lease KA, Doke JT, Tax FE, Walker JC . BAK1, an Arabidopsis LRR receptor-like protein kinase, interacts with BRI1 and modulates brassinosteroid signaling. Cell 2002; 110:213–222.

3. Chinchilla D, Zipfel C, Robatzek S, et al. A flagellin-induced complex of the receptor FLS2 and BAK1 initiates plant defence. Nature 2007; 448:497–500.

4. Zipfel C, Kunze G, Chinchilla D, et al. Perception of the bacterial PAMP EF-Tu by the receptor EFR restricts Agrobacterium-mediated transformation. Cell 2006; 125:749–760.

5. Wang X, Kota U, He K, et al. Sequential transphosphorylation of the BRI1/BAK1 receptor kinase complex impacts early events in brassinosteroid signaling. Dev Cell 2008; 15:220–235.

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