ArticleStress biology2024
Quantitative phosphoproteomics reveals molecular pathway network in wheat resistance to stripe rust.
Article in Stress biology, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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7 citing papers in PubMed.
- Wheat's war against stripe rust: Integrating host immunity, genomics and breeding for durable resistance.The plant genome · 2026Review
- Genome-Wide Identification of theBiology · 2026Article
- Wheat Plasma Membrane Receptors: Orchestrating Immunity and Bridging to Crop Improvement.Current issues in molecular biology · 2025Review
- Cellulose synthase TaCESA7 negatively regulates wheat resistance to stripe rust by reducing cell wall lignification.Stress biology · 2025Article
- Evolutionary characteristics, expression patterns of wheat receptor-like kinases and functional analysis of TaCrRLK1L16.Stress biology · 2025Article
- Transcriptomic-proteomic analysis reveals the regulatory mechanisms of Alfalfa (Frontiers in plant science · 2025Article
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11 authors.
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Abstract
Protein phosphorylation plays an important role in immune signaling transduction in plant resistance to pathogens. Wheat stripe rust, caused by Puccinia striiformis f. sp. tritici (Pst), severely devastates wheat production. Nonetheless, the molecular mechanism of wheat resistance to stripe rust remains limited. In this study, quantitative phosphoproteomics was employed to investigate the protein phosphorylation changes in wheat challenged by Pst. A total of 1537 and 2470 differentially accumulated phosphoproteins (DAPs) were identified from four early infection stage (6, 12, 18 and 24 h post-inoculation) in incompatible and compatible wheat-Pst interactions respectively. KEGG analysis revealed that Oxidative Phosphorylation, Phosphatidylinositol Signaling, and MAPK signaling processes are distinctively enriched in incompatible interaction, while Biosynthesis of secondary metabolites and RNA degradation process were significantly enriched in compatible interactions. In particular, abundant changes in phosphorylation levels of chloroplast proteins were identified, suggesting the regulatory role of photosynthesis in wheat-Pst interaction, which is further emphasized by protein-protein interaction (PPI) network analysis. Motif-x analysis identified [xxxxSPxxxx] motif, likely phosphorylation sites for defensive response-related kinases, and a new [xxxxSSxxxx] motif significantly enriched in incompatible interaction. The results shed light on the early phosphorylation events contributing to wheat resistance against Pst. Moreover, our study demonstrated that the phosphorylation levels of Nucleoside diphosphate kinase TaNAPK1 are upregulated at 12 hpi with CYR23 and at 24 hpi with CYR31. Transient silencing of TaNAPK1 was able to attenuate wheat resistance to CYR23 and CYR31. Our study provides new insights into the mechanisms underlying Pst-wheat interactions and may provide database to find potential targets for the development of new resistant varieties.
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