Abstract
Biotic stress factors pose a major threat to plant health and can significantly deteriorate plant productivity by impairing the physiological functions of the plant. To combat the wide range of pathogens and insect herbivores, plants deploy converging signaling pathways, where counteracting activities of protein kinases and phosphatases form a basic mechanism for determining appropriate defensive measures. Recent studies have identified Protein Phosphatase 2A (PP2A) as a crucial component that controls pathogenesis responses in various plant species. Genetic, proteomic and metabolomic approaches have underscored the versatile nature of PP2A, which contributes to the regulation of receptor signaling, organellar signaling, gene expression, metabolic pathways, and cell death, all of which essentially impact plant immunity. Associated with this, various PP2A subunits mediate post-translational regulation of metabolic enzymes and signaling components. Here we provide an overview of protein kinase/phosphatase functions in plant immunity signaling, and position the multifaceted functions of PP2A in the tightly inter-connected regulatory network that controls the perception, signaling and responding to biotic stress agents in plants.
Highlights
Modern agricultural practices and breeding programs have significantly increased crop yields over the past century
Phosphorelay Signaling from the Plasma Membrane to the Nucleus. Plants monitor their biotic environment through plasma membrane pattern recognition receptors, which act as receptorlike kinases (RLKs) or receptor-like proteins (RLPs) (Jones and Dangl, 2006; Gust and Felix, 2014) that can sense the presence of conserved pathogen-associated molecular patterns (PAMPs), such as bacterial flagella and peptidoglycans, the fungal cell wall constituent chitin or the saliva of aphids (Gómez-Gómez and Boller, 2000; Liu et al, 2012; Prince et al, 2014; Zipfel, 2014; Figure 1)
An example of a regulatory kinase–phosphatase interaction was provided by Bartels et al (2009), who showed that the dualspecificity phosphatase MAP KINASE PHOSPHATASE1 (MKP1), together with the PROTEIN TYROSINE PHOSPHATASE1 (PTP1) regulate the phosphorylation status and the activity of MPK6
Summary
Modern agricultural practices and breeding programs have significantly increased crop yields over the past century. Identification of stress-inducible biosynthetic pathways and modeling their integration with the metabolic and regulatory networks governing basic production, stress resistance and growth are increasing trends in modern plant biology (Allahverdiyeva et al, 2015). In these interactions, reversible protein phosphorylation, catalyzed by counteracting activities of protein kinases and protein phosphatases, connects stress perception and the immediate down-stream cascades with the signaling networks that regulate gene expression profiles and metabolic activities in the cell (Uhrig et al, 2013; van Wijk et al, 2014). SENSING AND SIGNALING OF PATHOGEN INFECTION: JOINT ACTION AMONG DIFFERENT CELLULAR COMPARTMENTS
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