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Cell Host Microbe. 2018 Feb 14;23(2):241-253.e6. doi: 10.1016/j.chom.2017.12.005. Epub 2018 Feb 3.

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

Author information

1
State Key Laboratory of Biocontrol, Guangdong Provincial Key Laboratory of Plant Resources, School of Life Sciences, Sun Yat-sen University, Guangzhou, Guangdong 510275, China.
2
State Key Laboratory of Biocontrol, Guangdong Provincial Key Laboratory of Plant Resources, School of Life Sciences, Sun Yat-sen University, Guangzhou, Guangdong 510275, China. Electronic address: lijfeng3@mail.sysu.edu.cn.
3
State Key Laboratory of Biocontrol, Guangdong Provincial Key Laboratory of Plant Resources, School of Life Sciences, Sun Yat-sen University, Guangzhou, Guangdong 510275, China. Electronic address: wanghb@mail.sysu.edu.cn.
4
State Key Laboratory of Biocontrol, Guangdong Provincial Key Laboratory of Plant Resources, School of Life Sciences, Sun Yat-sen University, Guangzhou, Guangdong 510275, China. Electronic address: lsswjf@mail.sysu.edu.cn.

Abstract

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 tyrosine428 (Tyr428), 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 phosphatase 1 (CIPP1), a predicted Ser/Thr phosphatase, to dephosphorylate Tyr428 and dampen CERK1 signaling. CIPP1 subsequently dissociates from Tyr428-dephosphorylated CERK1, allowing CERK1 to regain Tyr428 autophosphorylation and return to a standby state. This work sheds light onto plant chitin signaling and shows that a receptor kinase and phosphatase can coordinately regulate signal transduction of a receptor kinase through a phosphorylation cycle.

KEYWORDS:

dual specificity; phosphatase; plant chitin signaling; receptor kinase; tyrosine phosphorylation

PMID:
29396039
DOI:
10.1016/j.chom.2017.12.005
[Indexed for MEDLINE]
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