ArticleJournal of integrative plant biology2025
Maintaining basal B-RAF kinase activity for abscisic acid signaling via reciprocal phosphoregulation of a single serine residue.
Article in Journal of integrative plant biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 papers.
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Who cites it
5 citing papers in PubMed.
- A RAF-SnRK2-PP2C functional module regulates cell survival in the chlorophyte Chlamydomonas reinhardtii.The New phytologist · 2026Article
- Integrating molecular networks and physiological adaptation for heat-resilient crops.Journal of integrative plant biology · 2026Review
- Dynamic and Basal Phosphorylation Landscapes of Abscisic Acid Signaling Revealed by Phosphoproteome Analysis in Arabidopsis.International journal of molecular sciences · 2026Article
- Genome-Wide Identification and Hormone-Induced Expression Analysis of the Anthocyanidin Reductase Gene Family in Sainfoin (International journal of molecular sciences · 2025Article
- Maintaining basal B-RAF kinase activity for abscisic acid signaling via reciprocal phosphoregulation of a single serine residue.Journal of integrative plant biology · 2025Article
Corrections and comments
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Authors and funding
9 authors.
Funding
Abstract
The phytohormone abscisic acid (ABA) regulates plant responses to environmental stresses, development, and immunity. Under unfavorable conditions, ABA forms a complex with its receptor proteins Pyrabactin Resistance 1 (PYR1)/PYR1-likes (PYLs)/Regulatory Component of ABA Receptors (RCARs), inhibiting Clade A Protein Phosphatases Type 2C (PP2Cs) and releasing Sucrose Non-Fermenting-1-Related Protein Kinase 2s (SnRK2s) from PP2C-mediated inhibition. Rapidly Accelerated Fibrosarcoma (RAF) kinases from the B1, B2, and B3 subgroups phosphorylate and reactivate SnRK2s, initiating ABA responses. While ABA does not significantly activate B-RAFs, their basal activity is essential for initiating ABA signaling. However, the mechanisms sustaining this basal B-RAF activity are not fully understood. In this study, we revealed that Clade A PP2Cs interact with and dephosphorylate a certain number of B3 subgroup RAFs at a conserved serine residue, corresponding to Ser619 in RAF3, within the phosphate-binding loop. A phosphomimicking mutation at this residue, RAF3
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