Specific threonine phosphorylation of a host target by two unrelated type III effectors activates a host innate immune receptor in plants.
Specific threonine phosphorylation of a host target by two unrelated type III effectors activates a host innate immune receptor in plants.
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DOI：
10.1016/j.chom.2011.01.009
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发表时间：
2011-02-17
影响因子：
30.3
通讯作者：
Dangl JL
中科院分区：
文献类型：
--
作者：
Chung EH;da Cunha L;Wu AJ;Gao Z;Cherkis K;Afzal AJ;Mackey D;Dangl JL
拟南芥NB-LRR免疫受体RPM 1识别假单胞菌III型效应子AvrB或AvrRpm 1以产生免疫应答。虽然这两种效应子本身都不是激酶，但已知AvrRpm 1和AvrB靶向拟南芥RIN 4（一种基础植物防御的负调节因子）进行磷酸化。我们发现，RIN 4磷酸化激活RPM 1。RIN 4142 -176是必需的，并且具有适当的定位序列，足以支持效应子触发的RPM 1激活，其中位置166处的苏氨酸残基是关键的。T166的拟磷酸化取代导致效应子非依赖性RPM 1激活。RIN 4 T166在AvrB或AvrRpm 1存在下在体内被磷酸化。失去与AvrB相互作用的RIN 4突变体不能与RPM 1共免疫沉淀。这定义了一个共同的相互作用平台所需的RPM 1激活磷酸化的RIN 4响应致病效应。所有RIN 4样蛋白中类似的苏氨酸的保守性表明该残基的关键功能超出了RPM 1的调节。
The Arabidopsis NB-LRR immune receptor RPM1 recognizes the Pseudomonas syringae type III effectors AvrB or AvrRpm1 to mount an immune response. Although neither effector is itself a kinase, AvrRpm1 and AvrB are known to target Arabidopsis RIN4, a negative regulator of basal plant defense, for phosphorylation. We show that RIN4 phosphorylation activates RPM1. RIN4142–176 is necessary, and with appropriate localization sequences, sufficient to support effector-triggered RPM1 activation, with the threonine residue at position 166 being critical. Phosphomimic substitutions at T166 cause effector-independent RPM1 activation. RIN4 T166 is phosphorylated in vivo in the presence of AvrB or AvrRpm1. RIN4 mutants that lose interaction with AvrB cannot be co-immunoprecipitated with RPM1. This defines a common interaction platform required for RPM1 activation by phosphorylated RIN4 in response to pathogenic effectors. Conservation of an analogous threonine across all RIN4-like proteins suggests a key function for this residue beyond the regulation of RPM1.
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