S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signalling
S-acylation stabilizes ligand-induced receptor kinase complex formation during plant pattern-triggered immune signalling
复制标题
S-酰化在植物模式触发的免疫信号传导过程中稳定配体诱导的受体激酶复合物的形成
DOI：
10.1101/2021.08.30.457756
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发表时间：
2021
期刊：
影响因子：
--
通讯作者：
Hurst C
中科院分区：
文献类型：
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作者：
Hurst C
植物受体激酶是细胞外刺激的关键转换器，例如有益或致病微生物或分泌的信号分子的存在。受体激酶受许多翻译后修饰的调节。1，2，3在这里，使用免疫受体激酶FLS 24和EFR，5我们表明，在所有植物受体激酶中保守的半胱氨酸的S-酰化对功能至关重要。S-酰化涉及将长链脂肪酸添加到蛋白质内的半胱氨酸残基上，改变其在膜环境中的生化特性和行为。6我们观察到FLS 2在C-末端激酶结构域半胱氨酸残基上的S-酰化，在其配体flg 22以BAK 1共受体和PUB 12/13泛素连接酶依赖性方式感知后几分钟内。我们证明，S-酰化是必不可少的FLS 2介导的免疫信号和细菌感染的抗性。类似地，突变EFR中相应的保守半胱氨酸残基抑制了elf 18触发的信号传导。使用显微镜、洗涤剂和天然膜DIBMA纳米盘分析未刺激和活化的含FLS 2的复合物表明，S-酰化稳定并促进活化的受体激酶复合物在质膜上的保留，以增加信号传导效率。
Plant receptor kinases are key transducers of extracellular stimuli, such as the presence of beneficial or pathogenic microbes or secreted signaling molecules. Receptor kinases are regulated by numerous post-translational modifications.1,2,3Here, using the immune receptor kinases FLS24and EFR,5we show that S-acylation at a cysteine conserved in all plant receptor kinases is crucial for function. S-acylation involves the addition of long-chain fatty acids to cysteine residues within proteins, altering their biochemical properties and behavior within the membrane environment.6We observe S-acylation of FLS2 at C-terminal kinase domain cysteine residues within minutes following the perception of its ligand, flg22, in a BAK1 co-receptor and PUB12/13 ubiquitin ligase-dependent manner. We demonstrate that S-acylation is essential for FLS2-mediated immune signaling and resistance to bacterial infection. Similarly, mutating the corresponding conserved cysteine residue in EFR suppressed elf18-triggered signaling. Analysis of unstimulated and activated FLS2-containing complexes using microscopy, detergents, and native membrane DIBMA nanodiscs indicates that S-acylation stabilizes, and promotes retention of, activated receptor kinase complexes at the plasma membrane to increase signaling efficiency.