Regulation of ABA-Non-Activated SNF1-Related Protein Kinase 2 Signaling Pathways by Phosphatidic Acid

Autor: Justyna Maszkowska, Grażyna Goch, Maria Bucholc, Ewa Krzywińska, Maria Klimecka, Małgorzata Lichocka, Grażyna Dobrowolska, Jadwiga Szczegielniak
Jazyk: angličtina
Rok vydání: 2020
Předmět:
0106 biological sciences
0301 basic medicine
Arabidopsis thaliana
Arabidopsis
Pyruvate dehydrogenase phosphatase
01 natural sciences
lcsh:Chemistry
chemistry.chemical_compound
ERD14
Protein Interaction Maps
Phosphorylation
PP2CA
lcsh:QH301-705.5
Spectroscopy
SNF1-related protein kinases
Chemistry
Kinase
food and beverages
General Medicine
Phosphatidic acid
Computer Science Applications
Cell biology
phosphatidic acid
Signal transduction
Signal Transduction
PA
Phosphatase
Phosphatidic Acids
SnRK2-interacting calcium sensor
Protein Serine-Threonine Kinases
Article
Catalysis
Inorganic Chemistry
03 medical and health sciences
Physical and Theoretical Chemistry
dehydrins
Protein kinase A
Molecular Biology
Arabidopsis Proteins
SnRK2
Organic Chemistry
fungi
Subcellular localization
SCS
030104 developmental biology
lcsh:Biology (General)
lcsh:QD1-999
Abscisic Acid
010606 plant biology & botany
Zdroj: International Journal of Molecular Sciences, Vol 21, Iss 4984, p 4984 (2020)
International Journal of Molecular Sciences; Volume 21; Issue 14; Pages: 4984
International Journal of Molecular Sciences
ISSN: 1661-6596
1422-0067
Popis: 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.
Databáze: OpenAIRE
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