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A Tyrosine Phosphorylation Cycle Regulates Fungal Activation of a Plant Receptor Ser/Thr Kinase.

Cell Host Microbe. 2018; 
LiuJun,LiuBing,ChenSufen,GongBen-Qiang,ChenLijuan,ZhouQi,XiongFeng,WangMenglong,FengDongru,LiJian-Feng,WangHong-Bin,WangJ
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Catalog Antibody Rabbit Anti-GFP pAb GenScript Cat.#A01704; RRID: Get A Quote

摘要

Plants initiate immunity by cell-surface pattern-recognition receptors (PRRs), which perceive non-self molecules. PRRs are predominantly receptor serine/threonine (Ser/Thr) kinases that are evolutionarily related to animal interleukin-1 receptor-associated kinase (IRAK)/Pelle-soluble kinases. However, how the activity of these receptor kinases is modulated remains poorly understood. We report that the Arabidopsis PRR chitin elicitor receptor kinase 1 (CERK1) is autophosphorylated in unstimulated cells at tyrosine (Tyr), a modification that is required for CERK1 activation upon binding to the fungal cell wall component chitin. Upon chitin activation, CERK1 recruits the CERK1-interacting protein phosphata... More

关键词

dual specificity,phosphatase,plant chitin signaling,receptor kinase,tyrosine phosphoryla