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Regulation of ABA-Non-Activated SNF1-Related Protein Kinase 2 Signaling Pathways by Phosphatidic Acid
Maria Klimecka1,2, Maria Bucholc1, Justyna Maszkowska1
1Institute of Biochemistry and Biophysics, Polish Academy of Sciences, Pawińskiego 5a, 02-106 Warsaw, Poland.
International Journal of Molecular Sciences
|July 19, 2020
Summary
Phosphatidic acid (PA) regulates plant signaling by modulating ABA-non-activated SNF1-related protein kinases 2 (SnRK2s). PA affects SnRK2 activity, phosphorylation, and localization of key signaling partners, impacting plant responses.
Area of Science:
- Plant Biology
- Molecular Signaling
- Biochemistry
Background:
- Phosphatidic acid (PA) is crucial for plant growth, development, and environmental stress responses.
- SNF1-related protein kinases 2 (SnRK2s) are key signaling components, with some not activated by abscisic acid (ABA).
Purpose of the Study:
- To investigate the regulatory role of PA in ABA-non-activated SnRK2 signaling pathways.
- To elucidate how PA influences the activity, phosphorylation, and localization of SnRK2s and their interacting partners.
Main Methods:
- Investigated the effects of PA (specifically PA 16:0/18:1) on SnRK2 structure and target phosphorylation.
- Analyzed the impact of SnRK2 phosphorylation on dehydrin ERD14 interaction with PA and its localization.
- Assessed PA's modulation of protein phosphatase 2C (PP2C) activity and SnRK2-interacting calcium sensor function.
Main Results:
- PA 16:0/18:1 modulated SnRK2 structure and phosphorylation of targets like ERD14.
- Phosphorylation of ERD14 by SnRK2s affected its PA interaction and localization.
- PA inhibited the activity of phosphatases ABI1 and PP2CA, and modulated the localization/activity of a calcium sensor that regulates SnRK2s.
Conclusions:
- PA acts as a multi-level regulator of ABA-non-activated SnRK2 signaling.
- PA influences SnRK2 activity, phosphorylation status, and the localization of its cellular partners, including phosphatases and calcium sensors.
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