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Updated: Jun 30, 2025

Identification of Post-translational Modifications of Plant Protein Complexes
Published on: February 22, 2014
S-nitrosylation of a receptor-like cytoplasmic kinase regulates plant immunity
Beimi Cui1,2,3, Qiaona Pan3, Wenqiang Cui4,5
1Department of Plant Pathology, Key Laboratory of Agricultural Microbiology, College of Agriculture, Guizhou University, Guiyang, 550025, China.
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 Cys80. 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.
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