<i>S</i> -nitrosylation of a receptor-like cytoplasmic kinase regulates plant immunity-Reference-Cited by-同舟云学术

S -nitrosylation of a receptor-like cytoplasmic kinase regulates plant immunity

Published:2024-03-15 Issue:11 Volume:10 Page:
ISSN:2375-2548
Container-title:Science Advances
language:en
Short-container-title:Sci. Adv.

Author:

Cui Beimi¹²³^ORCID,Pan Qiaona³^ORCID,Cui Wenqiang⁴⁵^ORCID,Wang Yiqin⁴⁶^ORCID,Loake Verity I. P.⁷^ORCID,Yuan Shuguang⁵^ORCID,Liu Fengquan¹²^ORCID,Loake Gary J.³⁸^ORCID

Affiliation:

1. Department of Plant Pathology, Key Laboratory of Agricultural Microbiology, College of Agriculture, Guizhou University, Guiyang, 550025, China.

2. Institute of Plant Protection, Jiangsu Academy of Agricultural Sciences, Jiangsu Key Laboratory for Food Quality and Safety-State Key Laboratory Cultivation Base of Ministry of Science and Technology, Nanjing, 210014, China.

3. Institute of Molecular Plant Sciences, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3BF, UK.

4. University of Chinese Academy of Sciences, Beijing, 100049, China.

5. Institute of Biomedicine and Biotechnology, Shenzhen Institutes of Advanced Technology, Chinese Academy of Sciences, Shenzhen, 518055, China.

6. Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Beijing, 100101, China.

7. Faculty of Medicine, South Kensington Campus, Imperial College London, London, SW7 2AZ, UK.

8. Centre for Engineering Biology, School of Biological Sciences, University of Edinburgh, Edinburgh, EH9 3BF, UK.

Abstract

Perception of pathogen/microbial-associated molecular patterns (P/MAMPs) by plant cell surface receptors leads to a sustained burst of reactive oxygen species (ROS), a key feature of P/MAMP-triggered immunity (PTI). Here we report that P/MAMP recognition leads to a rapid nitrosative burst, initiating the accumulation of nitric oxide (NO), subsequently leading to S -nitrosylation of the receptor-like cytoplasmic kinase (RLCK), botrytis-induced kinase 1 (BIK1), at Cys 80 . This redox-based, posttranslational modification, promotes the phosphorylation of BIK1, subsequently resulting in BIK1 activation and stabilization. Further, BIK1 S -nitrosylation increases its physical interaction with RBOHD, the source of the apoplastic oxidative burst, promoting ROS formation. Our data identify mechanistic links between rapid NO accumulation and the expression of PTI, providing insights into plant immunity.

Publisher

American Association for the Advancement of Science (AAAS)

Link

https://www.science.org/doi/pdf/10.1126/sciadv.adk3126

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