Abstract
Protein phosphorylation plays a central role in the plant immune response signaling. PAMP signals induce rapid and transient phosphorylation of several proteins/enzymes involved in defense signaling system. The proteins that make up the signal transduction pathway are present in the cell prior to the perception of PAMP elicitor signal. On perception of the signal these proteins are activated by post-translational modifications and conformational changes induced by phosphorylation. Protein phosphorylation is carried out by different protein kinases. PAMP signals are perceived by plant pattern recognition receptors (PRRs), which belong to the family of receptor-like kinases (RLKs). The PAMPs have been shown to activate the RLKs by autophosphorylation by their own serine/threonine kinase. The autophosphorylation of the receptor kinases takes place within few seconds to few minutes after PAMP treatment and the autophosphorylated RLKs have been shown to be essential for PAMP signaling in plants. Calcium-dependent protein kinases (CDPKs) and mitogen-activated protein kinases (MAPKs) regulate expression of various enzymes involved in ROS, salicylate, jasmonate, ethylene, and abscisic acid signaling systems by inducing protein/enzyme phosphorylation. Protein kinase C is involved in phosphorylation of some transcription factors. His kinase family protein kinase takes part in ethylene signaling system. Protein dephosphorylation may also be involved in defense signaling and the phosphatases negatively regulate innate immune responses.
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Vidhyasekaran, P. (2014). Protein Phosphorylation and Dephosphorylation in Plant Immune Signaling Systems. In: PAMP Signals in Plant Innate Immunity. Signaling and Communication in Plants, vol 21. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-7426-1_9
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