Publications by authors named "Katarzyna Patrycja Szymanska"

SNF1-related protein kinase 2 s (SnRK2s) are major regulators of plant growth, development and responses to environmental stresses. Together with clade A protein phosphatases of type 2C (PP2C) and REGULATORY COMPONENTS OF ABA RECEPTOR (RCAR also known as PYRABACTIN RESISTANCE1 (PYR1) or PYR1-LIKE (PYL)) soluble abscisic acid (ABA) receptors they form the core of ABA-signaling. Clade A PP2Cs play a negative role in ABA signaling, primarily by inhibiting SnRK2 activity, through direct interaction and dephosphorylation of SnRK2s.

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Article Synopsis
  • SnRK2s are important proteins in plants that help manage responses to environmental stresses like osmotic stress and abscisic acid (ABA), which is crucial for signaling in these scenarios.
  • They serve as switches between promoting growth and responding to stress, requiring careful and temporary activation to function properly.
  • Although recent findings shed light on how SnRK2s are regulated, especially with ABA, there is still a significant lack of understanding regarding their regulation outside of ABA pathways.
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In response to salinity and various other environmental stresses, plants accumulate reactive oxygen species (ROS). The ROS produced at very early stages of the stress response act as signaling molecules activating defense mechanisms, whereas those produced at later stages in an uncontrolled way are detrimental to plant cells by damaging lipids, DNA, and proteins. Multiple systems are involved in ROS generation and also in ROS scavenging.

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Article Synopsis
  • - SnRK2s are protein kinases in plants that help manage responses to stress, particularly when water is scarce, and can be activated by osmotic stress or abscisic acid (ABA).
  • - The research focuses on SnRK2.10 from Arabidopsis thaliana, which is not activated by ABA but still plays a significant role in how plants react to salinity and dehydration.
  • - The study identified specific proteins (dehydrins ERD10 and ERD14) that SnRK2.10 phosphorylates under stress conditions, suggesting that this modification helps control where these proteins are located within the cell during stress responses.
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