ArticleProceedings of the National Academy of Sciences of the United States of America2011
Structural basis for basal activity and autoactivation of abscisic acid (ABA) signaling SnRK2 kinases.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 87 papers, 1 of them a synthesis that pooled it.
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Who cites it
87 citing papers in PubMed, 1 synthesis or guideline pooled it.
- Dry side of the core: a meta-analysis addressing the original nature of the ABA signalosome at the onset of seed imbibition.Frontiers in plant science · 2023Pooled it
- Guard cell signal transduction mechanisms controlling stomatal movements by light, abscisic acid, CO2, VPD and heat.Plant physiology · 2026Review
- A RAF-SnRK2-PP2C functional module regulates cell survival in the chlorophyte Chlamydomonas reinhardtii.The New phytologist · 2026Article
- An RGLG E3 Ubiquitin Ligase CaSIRE1 Negatively Regulates ABA-Dependent Drought Tolerance by Destabilizing CaSAP14 in Pepper.Plant, cell & environment · 2026Article
- The RCAR12-CAP1-OST1 module controls ABA-mediated stomatal closure in Arabidopsis.PLoS genetics · 2026Article
- Local peptide signalling induces stomatal closure under drought stress.Nature communications · 2025Article
- Protein Post-Translational Modifications in Plant Abiotic Stress Responses.Plants (Basel, Switzerland) · 2025Review
- The Pepper E3 Ligase CaGIR1 Acts as a Negative Regulator of Drought Response via Controlling CaGRAS1 Stability.Plant, cell & environment · 2025Article
- SnRK2 kinases sense molecular crowding and form condensates to disrupt ABI1 inhibition.Science advances · 2025Article
- Osmotic signaling releases PP2C-mediated inhibition of Arabidopsis SnRK2s via the receptor-like cytoplasmic kinase BIK1.The EMBO journal · 2024Article
- The Discovery of Highly Efficient and Promising ABA Receptor Antagonists for Agricultural Applications Based on APAn Modification.Molecules (Basel, Switzerland) · 2024Article
- OPEN STOMATA 1 phosphorylates CYCLIC NUCLEOTIDE-GATED CHANNELs to trigger Ca2+ signaling for abscisic acid-induced stomatal closure in Arabidopsis.The Plant cell · 2024Article
- The Modulation of Sucrose Nonfermenting 1-Related Protein Kinase 2.6 State by Persulfidation and Phosphorylation: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2023Article
- Persistence of Abscisic Acid Analogs in Plants: Chemical Control of Plant Growth and Physiology.Genes · 2023Review
- Genome-wide investigation of SnRK2 gene family in two jute species: Corchorus olitorius and Corchorus capsularis.Journal, genetic engineering & biotechnology · 2023Article
- Characterization and expression analysis of SnRK2, PYL, and ABF/ AREB/ ABI5 gene families in sweet potato.PloS one · 2023Article
- Identification and characteristics of SnRK genes and cold stress-induced expression profiles in Liriodendron chinense.BMC genomics · 2022Article
- Article
- Genome-Wide Identification, Expression Pattern and Sequence Variation Analysis ofPlants (Basel, Switzerland) · 2022Article
- Article
27 more citing papers are in PubMed but not listed here.
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Authors and funding
13 authors.
Funding
Abstract
Abscisic acid (ABA) is an essential hormone that controls plant growth, development, and responses to abiotic stresses. Central for ABA signaling is the ABA-mediated autoactivation of three monomeric Snf1-related kinases (SnRK2.2, -2.3, and -2.6). In the absence of ABA, SnRK2s are kept in an inactive state by forming physical complexes with type 2C protein phosphatases (PP2Cs). Upon relief of this inhibition, SnRK2 kinases can autoactivate through unknown mechanisms. Here, we report the crystal structures of full-length Arabidopsis thaliana SnRK2.3 and SnRK2.6 at 1.9- and 2.3-Å resolution, respectively. The structures, in combination with biochemical studies, reveal a two-step mechanism of intramolecular kinase activation that resembles the intermolecular activation of cyclin-dependent kinases. First, release of inhibition by PP2C allows the SnRK2s to become partially active because of an intramolecular stabilization of the catalytic domain by a conserved helix in the kinase regulatory domain. This stabilization enables SnRK2s to gain full activity by activation loop autophosphorylation. Autophosphorylation is more efficient in SnRK2.6, which has higher stability than SnRK2.3 and has well-structured activation loop phosphate acceptor sites that are positioned next to the catalytic site. Together, these data provide a structural framework that links ABA-mediated release of PP2C inhibition to activation of SnRK2 kinases.
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