Quantitative Phosphoproteomics of Early Elicitor Signaling in Arabidopsis*S

By J. Benschop, S. Mohammed, Martina C O'Flaherty, Albert J. R. Heck, M. Slijper, Frank L. H. Menke. Molecular & Cellular Proteomics, 2007

652 citations recorded by the source corpus.

Perception of general elicitors by plant cells initiates signal transduction cascades that are regulated by protein phosphorylation. The earliest signaling events occur within minutes and include ion fluxes across the plasma membrane, activation of MAPKs, and the formation of reactive oxygen species. The phosphorylation events that regulate these signaling cascades are largely unknown. Here we present a mass spectrometry-based quantitative phosphoproteomics approach that identified differentially phosphorylated sites in signaling and response proteins from Arabidopsis cells treated with either flg22 or xylanase. Our approach was sensitive enough to quantitate phosphorylation on low abundance signaling proteins such as calcium-dependent protein kinases and receptor-like kinase family members. With this approach we identified one or more differentially phosphorylated sites in 76 membrane-associated proteins including a number of defense-related proteins. Our data on phosphorylation indicate a high degree of complexity at the level of post-translational modification as exemplified by the complex modification patterns of respiratory burst oxidase protein D. Furthermore the data also suggest that protein translocation and vesicle traffic are important aspects of early signaling and defense in response to general elicitors. Our study presents the largest quantitative Arabidopsis phosphoproteomics data set to date and provides a new resource that can be used to gain novel insight into plant defense signal transduction and early defense response.

Subfields: Molecular Biology, Plant Science

View Paper: https://www.semanticscholar.org/paper/124057bc6ead4346972bd2fedb3c2a98eb08bdc9

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Citations in the corpus

Antagonistic regulation of PIN phosphorylation by PP2A and PINOID directs auxin flux. (2007, result): “These results together with previous reports (Nühse et al., 2004; Benschop et al., 2007) demonstrate that PIN1 and possibly also other PIN proteins are phosphorylated in their central hydrophilic loop in Arabidopsis.”
Brassinosteroid signal transduction from cell surface receptor kinases to nuclear transcription factors (2009, background): “BSL1 and its two other homologues have all been identified as plasma membrane proteins by recent proteomics studie”
Calcium-dependent protein kinase/NADPH oxidase activation circuit is required for rapid defense signal propagation (2013, background): “MS analysis has revealed that the RBOHD protein becomes phosphorylated in response to the bacterial PAMP molecule flagellin in vivo (23, 24).”
Proline Metabolism and Its Implications for Plant-Environment Interaction (2010, background): “Phosphorylation of P5CS1 has been found in large scale proteomics studies (Benschop et al., 2007; Reiland et al., 2009) but its significance in regulating P5CS1 activity is not known.”
Direct regulation of the NADPH oxidase RBOHD by the PRR-associated kinase BIK1 during plant immunity. (2014, background): “PAMP treatment induces within 10 min the phosphorylation of the RBOHD residues S39, S148, S152, S163, S343, and S347 (Benschop et al., 2007; Nühse et al., 2007; Dubiella et al., 2013).”
The FLS2-associated kinase BIK1 directly phosphorylates the NADPH oxidase RbohD to control plant immunity. (2014, background): “Phosphoproteomic studies have shown that RbohD is phosphorylated at multiple sites required for the FLS2-mediated ROS production (Benschop et al., 2007; Nühse et al., 2007).”
A receptor-like cytoplasmic kinase, BIK1, associates with a flagellin receptor complex to initiate plant innate immunity (2009, background): “Although some phosphorylated proteins have been identified in response toMAMPtreatment, their exactmodeof action inMAMP signaling has remained elusive (19, 20).”
Signaling mechanisms in pattern-triggered immunity (PTI). (2015, background): “allowed to precisely identify some of the protein phosphorylation sites (Benschop et al., 2007; Nuhse et al., 2007; Mithoe et al., 2012; Rayapuram et al., 2014).”