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

• Published in: Cell research 2012-08, Vol.22 (8), p.1304-1308
• Main Authors: Yan, Liming, Ma, Yuanyuan, Liu, Dan, Wei, Xiaochao, Sun, Yuna, Chen, Xiaoyue, Zhao, Huadong, Zhou, Jingwen, Wang, Zhiyong, Shui, Wenqing, Lou, Zhiyong
• Format: Article
• Language: English
• Subjects: 631/449/2169; 631/535; 631/80/458/1733; Arabidopsis - chemistry; Arabidopsis - enzymology; Arabidopsis Proteins - chemistry; Binding Sites; Biomedical and Life Sciences; Cell Biology; Enzyme Activation; Letter to the Editor; Life Sciences; Multiprotein Complexes - chemistry; Phosphorylation; Protein Kinases - chemistry; Protein Stability; Protein Structure, Tertiary; Protein-Serine-Threonine Kinases - chemistry; Structure-Activity Relationship; 受体植物; 受体激酶; 受体蛋白激酶; 富含亮氨酸重复序列; 激活; 磷酸化; 结构基础; 胞外结构域
• ISSN: 1001-0602; 1748-7838
• DOI: 10.1038/cr.2012.74

Dear Editor, Receptor-like kinases （RLKs） constitute the major family of cell surface-associated receptors in plants and play essential roles in perceiving extracellular signals [1]. Over two hundred members of the largest subfam- ily of RLKs that contain leucine-rich repeat extracellular domains （LRR-RLK） are found in Arabidopsis, among which BRIl-associated kinase 1 （BAK1） is one of the best studied. BAK1 was initially identified based on its association with the LRR-RLK BRI1, which perceives brassinosteroid, an important hormone that regulates a wide range of developmental and physiological processes in plants [2]. BAK1 also serves as a co-receptor for sev- eral other LRR-RLKs that perceive pathogen-associated molecular patterns （PAMPs）, including flagellin-sensing 2 （FLS2） and elongation factor EF-Tu receptor [3, 4], and is therefore required for the innate immunity of plants. The reciprocal phosphorylation on the cytoplas- mic domains of BAK1 and the ligand-binding RLKs in the complex is a prerequisite for the full activation of the receptor kinase [5]. The crystal structure of BAK1 com- plexed with AvrPtoB, which is an effector secreted by Pseudomonas syringae pv. Tomato to suppress PAMP- triggered immunity, recently revealed the mechanism by which BAK1 activity is inhibited [6]. However, the mechanism for BAK1 activation, particularly the impact of phosphorylation of key residues on BAK1 activation, remains unclear.