Direct Regulation of the NADPH Oxidase RBOHD by the PRR-Associated Kinase BIK1 during Plant Immunity
Direct Regulation of the NADPH Oxidase RBOHD by the PRR-Associated Kinase BIK1 during Plant Immunity
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DOI：
10.1016/j.molcel.2014.02.021
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发表时间：
2014-04-10
期刊：
影响因子：
16
通讯作者：
Zipfel, Cyril
中科院分区：
文献类型：
--
作者：
Kadota, Yasuhiro;Sklenar, Jan;Zipfel, Cyril
活性氧簇（ROS）爆发的快速产生是跨王国免疫中保守的信号输出。在植物中，通过表面定位的模式识别受体（PRR）感知病原体相关分子模式（PAMP）通过迄今未知的机制激活NADPH氧化酶RBOHD。在这里，我们表明，RBOHD存在于复杂的受体激酶EFR和FLS 2，这是细菌EF-Tu和鞭毛蛋白的PRRs，分别。质膜相关激酶BIK 1是PRR复合物的直接底物，在PAMP感知时直接与RBOHD相互作用并使其磷酸化。BIK 1磷酸化的残基与钙依赖性蛋白激酶不同，PAMP诱导的BIK 1活化和BIK 1介导的RBOHD磷酸化均不依赖于钙。重要的是，这些残基的磷酸化对于PAMP诱导的ROS爆发和抗菌免疫至关重要。我们的研究揭示了植物RBOH的快速调节机制，该机制与其典型的钙基调节平行发生并且是必不可少的。
The rapid production of reactive oxygen species (ROS) burst is a conserved signaling output in immunity across kingdoms. In plants, perception of pathogen- associated molecular patterns (PAMPs) by surface-localized pattern recognition receptors (PRRs) activates the NADPH oxidase RBOHD by hitherto unknown mechanisms. Here, we show that RBOHD exists in complex with the receptor kinases EFR and FLS2, which are the PRRs for bacterial EF-Tu and flagellin, respectively. The plasma-membrane-associated kinase BIK1, which is a direct substrate of the PRR complex, directly interacts with and phosphorylates RBOHD upon PAMP perception. BIK1 phosphorylates different residues than calcium-dependent protein kinases, and both PAMP-induced BIK1 activation and BIK1-mediated phosphorylation of RBOHD are calcium independent. Importantly, phosphorylation of these residues is critical for the PAMP-induced ROS burst and antibacterial immunity. Our study reveals a rapid regulatory mechanism of a plant RBOH, which occurs in parallel with and is essential for its paradigmatic calcium-based regulation.