Differential phosphorylation of receptor kinase SlLYK4 mediates immune responses to bacterial and fungal pathogens in tomato

IF 11.7 1区综合性期刊 Q1 MULTIDISCIPLINARY SCIENCES

Science Advances Pub Date : 2025-05-30 DOI:10.1126/sciadv.adu2840

Wanting Zhu, Sen Cao, Mengling Huang, Pengyue Li, Jingjing Ke, Ai Xu, Yang Lin, Jiatao Xie, Jiasen Cheng, Yanping Fu, Daohong Jiang, Xiao Yu, Bo Li

{"title":"Differential phosphorylation of receptor kinase SlLYK4 mediates immune responses to bacterial and fungal pathogens in tomato","authors":"Wanting Zhu, Sen Cao, Mengling Huang, Pengyue Li, Jingjing Ke, Ai Xu, Yang Lin, Jiatao Xie, Jiasen Cheng, Yanping Fu, Daohong Jiang, Xiao Yu, Bo Li","doi":"10.1126/sciadv.adu2840","DOIUrl":null,"url":null,"abstract":"<div >Bacterial wilt caused by <i>Ralstonia solanacearum</i> is a devastating plant disease. Exopolysaccharide (EPS), a major virulence factor of <i>R. solanacearum</i>, elicits pattern-triggered immunity (PTI) in tomato, but the means by which EPS is recognized in the plant remain poorly understood. We found that tomato non-arginine-aspartate (non-RD) receptor kinase SlLYK4 mediates the perception of <i>R. solanacearum</i> EPS and positively regulates resistance to bacterial wilt. The RD receptor kinases SlLYK1 and SlLYK13 are required for EPS-triggered immune responses and form complexes with SlLYK4. These receptor kinase complexes have dual functions in recognizing bacterial EPS and fungal chitin. Phosphorylation of serine-320 in the juxtamembrane domain of SlLYK4 is essential in EPS- and chitin-mediated signaling, whereas phosphorylation of serine-334 or serine-634 in the C-terminal domain is required for chitin or EPS signaling, respectively. Our results reveal the mechanism underlying EPS recognition in tomato and provide insight into how differential phosphorylation of receptor kinase regulates antibacterial and antifungal immunity.</div>","PeriodicalId":21609,"journal":{"name":"Science Advances","volume":"11 22","pages":""},"PeriodicalIF":11.7000,"publicationDate":"2025-05-30","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.science.org/doi/reader/10.1126/sciadv.adu2840","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Science Advances","FirstCategoryId":"103","ListUrlMain":"https://www.science.org/doi/10.1126/sciadv.adu2840","RegionNum":1,"RegionCategory":"综合性期刊","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"MULTIDISCIPLINARY SCIENCES","Score":null,"Total":0}

引用次数: 0

Abstract

Bacterial wilt caused by Ralstonia solanacearum is a devastating plant disease. Exopolysaccharide (EPS), a major virulence factor of R. solanacearum, elicits pattern-triggered immunity (PTI) in tomato, but the means by which EPS is recognized in the plant remain poorly understood. We found that tomato non-arginine-aspartate (non-RD) receptor kinase SlLYK4 mediates the perception of R. solanacearum EPS and positively regulates resistance to bacterial wilt. The RD receptor kinases SlLYK1 and SlLYK13 are required for EPS-triggered immune responses and form complexes with SlLYK4. These receptor kinase complexes have dual functions in recognizing bacterial EPS and fungal chitin. Phosphorylation of serine-320 in the juxtamembrane domain of SlLYK4 is essential in EPS- and chitin-mediated signaling, whereas phosphorylation of serine-334 or serine-634 in the C-terminal domain is required for chitin or EPS signaling, respectively. Our results reveal the mechanism underlying EPS recognition in tomato and provide insight into how differential phosphorylation of receptor kinase regulates antibacterial and antifungal immunity.

Abstract Image

查看原文本刊更多论文

受体激酶SlLYK4的差异磷酸化介导番茄对细菌和真菌病原体的免疫反应

青枯病（Ralstonia solanacearum）是一种毁灭性的植物病害。外多糖（Exopolysaccharide， EPS）是番茄红霉（R. solanacearum）的主要毒力因子，可引起番茄的模式触发免疫（pattern-triggered immunity， PTI），但其在番茄中的识别途径尚不清楚。研究发现，番茄非精氨酸-天冬氨酸（non-RD）受体激酶SlLYK4介导番茄红枯菌对EPS的感知，并正调控其对青枯病的抗性。RD受体激酶SlLYK1和SlLYK13是eps触发的免疫应答所必需的，并与SlLYK4形成复合物。这些受体激酶复合物在识别细菌EPS和真菌几丁质方面具有双重功能。SlLYK4近膜域丝氨酸-320的磷酸化在EPS和几丁质介导的信号传导中是必需的，而c端域丝氨酸-334或丝氨酸-634的磷酸化分别是几丁质或EPS信号传导所必需的。我们的研究结果揭示了番茄中EPS识别的机制，并为受体激酶的差异磷酸化如何调节抗菌和抗真菌免疫提供了见解。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

求助全文

约1分钟内获得全文求助全文

来源期刊

Science Advances 综合性期刊-综合性期刊

CiteScore

21.40

自引率

1.50%

发文量

1937

审稿时长

29 weeks

期刊介绍： Science Advances, an open-access journal by AAAS, publishes impactful research in diverse scientific areas. It aims for fair, fast, and expert peer review, providing freely accessible research to readers. Led by distinguished scientists, the journal supports AAAS's mission by extending Science magazine's capacity to identify and promote significant advances. Evolving digital publishing technologies play a crucial role in advancing AAAS's global mission for science communication and benefitting humankind.