ArticleThe New phytologist2024
Subfamily C7 Raf-like kinases MRK1, RAF26, and RAF39 regulate immune homeostasis and stomatal opening in Arabidopsis thaliana.
Article in The New phytologist, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Review
- Decoding MAPK cascades in plant immunity: Activation, regulation, integration, and pathogen manipulation.Journal of integrative plant biology · 2026Review
- Arabidopsis Circadian Clock Protein CCA1 Negatively Regulates the Calcium-Binding Protein CCaP1 to Modulate Dark-Responsive Stomatal Movement.Plant, cell & environment · 2026Article
- Stomatal CO2 sensing in plants: control of gas exchange and interactions with environmental stimuli.Plant & cell physiology · 2025Review
- Catalytically inactive subgroup VIII receptor-like cytoplasmic kinases regulate the immune-triggered oxidative burst in Arabidopsis thaliana.Journal of experimental botany · 2025Article
- Biological functionality of non-functional protein kinases.Journal of experimental botany · 2025Article
- Phosphorylation of PIP2;7 by CPK28 or Phytophthora kinase effectors dampens pattern-triggered immunity in Arabidopsis.Plant communications · 2025Article
- Article
Corrections and comments
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Authors and funding
14 authors.
Funding
Abstract
The calcium-dependent protein kinase CPK28 regulates several stress pathways in multiple plant species. Here, we aimed to discover CPK28-associated proteins in Arabidopsis thaliana. We used affinity-based proteomics and identified several potential CPK28 binding partners, including the C7 Raf-like kinases MRK1, RAF26, and RAF39. We used biochemistry, genetics, and physiological assays to gain insight into their function. We define redundant roles for these kinases in stomatal opening, immune-triggered reactive oxygen species (ROS) production, and resistance to a bacterial pathogen. We report that CPK28 associates with and trans-phosphorylates RAF26 and RAF39, and that MRK1, RAF26, and RAF39 are active kinases that localize to endomembranes. Although Raf-like kinases share some features with mitogen-activated protein kinase kinase kinases (MKKKs), we found that MRK1, RAF26, and RAF39 are unable to trans-phosphorylate any of the 10 Arabidopsis mitogen-activated protein kinase kinases (MKKs). Overall, our study suggests that C7 Raf-like kinases associate with and are phosphorylated by CPK28, function redundantly in stomatal opening and immunity, and possess substrate specificities distinct from canonical MKKKs.
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Registered trials
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