ArticleBMC plant biology2016
Substrate thiophosphorylation by Arabidopsis mitogen-activated protein kinases.
Article in BMC plant biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- STUB1-induced polyubiquitination of SIK3 in alveolar type 2 epithelial cells alleviates severity and outcomes of acute lung injury.Cell death & disease · 2026Article
- Mitogen-Activated Protein Kinases 3/6 Reduce Auxin Signaling via Stabilizing Indoleacetic Acid-Induced Proteins 8/9 in Plant Abiotic Stress Adaptation.International journal of molecular sciences · 2025Article
- The Arabidopsis thaliana onset of leaf death 12 mutation in the lectin receptor kinase P2K2 results in an autoimmune phenotype.BMC plant biology · 2023Article
- Auxin promotes hypocotyl elongation by enhancing BZR1 nuclear accumulation inScience advances · 2023Article
- Article
- A New Approach for Wounding Research: MYC2 Gene Expression and Protein Stability in WoundedPlants (Basel, Switzerland) · 2021Article
- The mitogen-activated protein kinase 4-phosphorylated heat shock factor A4A regulates responses to combined salt and heat stresses.Journal of experimental botany · 2019Article
- A chemical genetic approach to engineer phototropin kinases for substrate labeling.The Journal of biological chemistry · 2018Article
- Cellular Complexity in MAPK Signaling in Plants: Questions and Emerging Tools to Answer Them.Frontiers in plant science · 2018Review
- ABA-Induced Stomatal Closure Involves ALMT4, a Phosphorylation-Dependent Vacuolar Anion Channel of Arabidopsis.The Plant cell · 2017Article
- CombinedFrontiers in plant science · 2017Article
- Modulation of plant growth in vivo and identification of kinase substrates using an analog-sensitive variant of CYCLIN-DEPENDENT KINASE A;1.BMC plant biology · 2016Article
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundMitogen-activated protein kinase (MPK) cascades are important to cellular signaling in eukaryotes. They regulate growth, development and the response to environmental challenges. MPK cascades function via reversible phosphorylation of cascade components, MEKK, MEK, and MPK, but also by MPK substrate phosphorylation. Using mass spectrometry, we previously identified many in vivo MPK3 and MPK6 substrates in Arabidopsis thaliana, and we disclosed their phosphorylation sites.
resultsWe verified phosphorylation of several of our previously identified MPK3/6 substrates using a nonradioactive in vitro labeling assay. We engineered MPK3, MPK4, and MPK6 to accept bio-orthogonal ATPγS analogs for thiophosphorylating their appropriate substrate proteins. Subsequent alkylation of the thiophosphorylated amino acid residue(s) allows immunodetection using thiophosphate ester-specific antibodies. Site-directed mutagenesis of amino acids confirmed the protein substrates' site-specific phosphorylation by MPK3 and MPK6. A combined assay with MPK3, MPK6, and MPK4 revealed substrate specificity of the individual kinases.
conclusionOur work demonstrates that the in vitro-labeling assay represents an effective, specific and highly sensitive test for determining kinase-substrate relationships.
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