Details

Autor(en) / Beteiligte

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

Titel

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

Ist Teil von

• Cell research, 2012-08, Vol.22 (8), p.1304-1308

Ort / Verlag

London: Nature Publishing Group UK

Erscheinungsjahr

2012

Quelle

MEDLINE

Beschreibungen/Notizen

• 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.