Abstract
Plant stress implies a series of processes and states where growth and development conditions are extremely different from optimal ones. Numerous data indicate that plant response to stress is strongly associated with changes in protein phosphorylation state under all known stress factors and extracellular signals. Self-incompatibility, initiation of mitosis, isoprenoid biosynthesis, cytoplasmic streaming, sucrose phosphate synthase activity, MSERK1 activity and phosphoenolpyruvate carboxylase activity are the examples of regulation of cellular responses that involved different protein kinases and protein phosphatases. Another feature of protein phosphatase is regulation, which underlies the mutual relationship between the type of a biotic stress factor and different regulating subunits. Here we present a brief overview of current experimental data on the role of plant phosphatases in stress, with an emphasis on tyrosine protein phosphatases (PTP1, DSPsI, MKPs) and Ser/Thr protein phosphatases of types PP1, PP2 and PP2C, especially with regard to cytoskeletal regulation.
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Samofalova, D.O., Karpov, P.A., Raevsky, A.V., Blume, Y.B. (2020). Interplay of Protein Phosphatases with Cytoskeleton Signaling in Response to Stress Factors in Plants. In: Pandey, G.K. (eds) Protein Phosphatases and Stress Management in Plants. Springer, Cham. https://doi.org/10.1007/978-3-030-48733-1_14
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