A Tyrosine Phosphorylation Cycle Regulates Fungal Activation of a Plant Receptor Ser/Thr Kinase
A Tyrosine Phosphorylation Cycle Regulates Fungal Activation of a Plant Receptor Ser/Thr Kinase
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DOI：
10.1016/j.chom.2017.12.005
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发表时间：
2018-02-14
影响因子：
30.3
通讯作者：
Wang, Jinfa
中科院分区：
文献类型：
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作者：
Liu, Jun;Liu, Bing;Wang, Jinfa
植物通过细胞表面模式识别受体（PRRs）启动免疫，PRRs感知非自我分子。PRR主要是与动物白细胞介素-1受体相关激酶（IRAK）/Pelle可溶性激酶进化相关的受体丝氨酸/苏氨酸（Ser/Thr）激酶。然而，这些受体激酶的活性是如何调节的仍然知之甚少。我们报告说，拟南芥PRR几丁质诱导受体激酶1（CERK 1）在未受刺激的细胞中酪氨酸（428）（Tyr（428））自磷酸化，这是一种修饰，需要CERK 1激活后结合到真菌细胞壁组分几丁质。在几丁质活化后，CERK 1募集CERK 1相互作用蛋白磷酸酶1（CIPP 1），一种预测的Ser/Thr磷酸酶，使Tyr（428）去磷酸化并抑制CERK 1信号传导。CIPP 1随后从Tyr（428）-去磷酸化的CERK 1解离，使CERK 1重新获得Tyr（428）自磷酸化并返回备用状态。这项工作揭示了植物几丁质信号转导，并表明受体激酶和磷酸酶可以协调调节受体激酶通过磷酸化循环的信号转导。
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(428) (Tyr(428)), 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 Tyr(428) and dampen CERK1 signaling. CIPP1 subsequently dissociates from Tyr(428)-dephosphorylated CERK1, allowing CERK1 to regain Tyr(428) 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.