ArticleInternational journal of molecular sciences2020
Regulation of ABA-Non-Activated SNF1-Related Protein Kinase 2 Signaling Pathways by Phosphatidic Acid.
Article in International journal of molecular sciences, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- Phytohormonal Regulation of Plant Responses to Major Abiotic Stresses: From Signaling Pathways to Hormonal Crosstalk.Metabolites · 2026Review
- A High-Thousand-Seed-Weight Mutant ofInternational journal of molecular sciences · 2026Article
- SnRK2s: Kinases or Substrates?Plants (Basel, Switzerland) · 2025Review
- Article
- Phosphatidic Acid in Plant Hormonal Signaling: From Target Proteins to Membrane Conformations.International journal of molecular sciences · 2022Review
- The network centered on ICEs play roles in plant cold tolerance, growth and development.Planta · 2022Review
- The Multifaceted Regulation of SnRK2 Kinases.Cells · 2021Review
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Authors and funding
8 authors at 1 institution in 1 country.
Funding
Abstract
Phosphatidic acid (PA) is involved in the regulation of plant growth and development, as well as responses to various environmental stimuli. Several PA targets in plant cells were identified, including two SNF1-related protein kinases 2 (SnRK2s), SnRK2.10 and SnRK2.4, which are not activated by abscisic acid (ABA). Here, we investigated the effects of PA on various elements of ABA-non-activated SnRK2 signaling. PA 16:0/18:1 was found to modulate the SnRK2 structure and the phosphorylation of some SnRK2 targets. Conversely, phosphorylation by the ABA-non-activated SnRK2s, of one of such targets, dehydrin Early Responsive to Dehydration 14 (ERD14), affects its interaction with PA and subcellular localization. Moreover, PA 16:0/18:1 modulates the activity and/or localization of negative regulators of the ABA-non-activated SnRK2s, not only of the ABA insensitive 1 (ABI1) phosphatase, which was identified earlier, but also of another protein phosphatase 2C, PP2CA. The activity of both phosphatases was inhibited by about 50% in the presence of 50 μM PA. PA 16:0/18:1 also impacts the phosphorylation and subcellular localization of SnRK2-interacting calcium sensor, known to inhibit SnRK2 activity in a calcium-dependent manner. Thus, PA was found to regulate ABA-non-activated SnRK2 signaling at several levels: the activity, phosphorylation status and/or localization of SnRK2 cellular partners.
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