ArticleJournal of experimental botany2016
Quantitative phosphoproteomics of protein kinase SnRK1 regulated protein phosphorylation in Arabidopsis under submergence.
Article in Journal of experimental botany, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 64 papers.
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Who cites it
64 citing papers in PubMed.
- Review
- Energy-sensing kinase OsSnRK1b and its regulator OsCTK1 promote chilling-induced stomatal closure and cold tolerance.Nature communications · 2026Article
- Nuclear SnRK1 Activity Delays Clubroot Development in Arabidopsis by Reducing Sink Strength.Plant, cell & environment · 2026Article
- Duet between sugars and hormones: The molecular dialogue fine-tuning hypoxia acclimation in plants.Journal of integrative plant biology · 2026Review
- Molecular and hormonal regulation of plant responses to waterlogging stress: From fundamental mechanisms to potential strategies for engineering crop tolerance.Plant communications · 2026Review
- FvMAPK6-Mediated FvMYB44s/FvSWEET1 Dual-Layer Regulation Modulates Sugar Accumulation in Strawberry Fruit, With FvSPS3 Enabling Quality-Yield Balance.Plant biotechnology journal · 2026Article
- The SnRK1-RAP2.4h-PIP2 module contributes to the trade-off between growth and hypoxia tolerance in plants.Nature communications · 2026Article
- Dynamic and Basal Phosphorylation Landscapes of Abscisic Acid Signaling Revealed by Phosphoproteome Analysis in Arabidopsis.International journal of molecular sciences · 2026Article
- Quantification of SnRK1.1 response through analysis of its intracellular distribution.Plant cell reports · 2026Article
- Integrated physiological, proteomic, and phosphoproteomic analyses of 24-epibrassinolide-mediated yield protection under complete submergence during panicle differentiation in rice.Frontiers in plant science · 2026Article
- Context-dependent coordination of TOR and SnRK1 signaling under carbon and nitrogen perturbations.Frontiers in plant science · 2026Article
- Cellular energy sensor SnRK1 suppresses salicylic acid-dependent and -independent defenses and bacterial resistance inProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Integrative Transcriptomic and Phosphoproteomic Analysis Reveals Key Components of the SnRK1 Signaling Network in Rice.Plant direct · 2025Article
- Perception and processing of stress signals by plant mitochondria.The Plant journal : for cell and molecular biology · 2024Review
- The lowdown on breakdown: Open questions in plant proteolysis.The Plant cell · 2024Review
- New Insights into the Connections between Flooding/Hypoxia Response and Plant Defenses against Pathogens.Plants (Basel, Switzerland) · 2024Review
- Molecular mechanism of trehalose 6-phosphate inhibition of the plant metabolic sensor kinase SnRK1.Science advances · 2024Article
- What, where, and how: Regulation of translation and the translational landscape in plants.The Plant cell · 2024Review
- ATP homeostasis and signaling in plants.Plant communications · 2024Review
- Coordination between two cis-elements of WRKY33, bound by the same transcription factor, confers humid adaption in Arabidopsis thaliana.Plant molecular biology · 2024Article
4 more citing papers are in PubMed but not listed here.
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4 authors.
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Abstract
SNF1 RELATED PROTEIN KINASE 1 (SnRK1) is proposed to be a central integrator of the plant stress and energy starvation signalling pathways. We observed that the Arabidopsis SnRK1.1 dominant negative mutant (SnRK1.1 (K48M) ) had lower tolerance to submergence than the wild type, suggesting that SnRK1.1-dependent phosphorylation of target proteins is important in signalling pathways triggered by submergence. We conducted quantitative phosphoproteomics and found that the phosphorylation levels of 57 proteins increased and the levels of 27 proteins decreased in Col-0 within 0.5-3h of submergence. Among the 57 proteins with increased phosphorylation in Col-0, 38 did not show increased phosphorylation levels in SnRK1.1 (K48M) under submergence. These proteins are involved mainly in sugar and protein synthesis. In particular, the phosphorylation of MPK6, which is involved in regulating ROS responses under abiotic stresses, was disrupted in the SnRK1.1 (K48M) mutant. In addition, PTP1, a negative regulator of MPK6 activity that directly dephosphorylates MPK6, was also regulated by SnRK1.1. We also showed that energy conservation was disrupted in SnRK1.1 (K48M) , mpk6, and PTP1 (S7AS8A) under submergence. These results reveal insights into the function of SnRK1 and the downstream signalling factors related to submergence.
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