{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Haj Ahmad F"],"funding":["Deutsche Forschungsgemeinschaft (DFG)","Deutscher Akademischer Austauschdienst (DAAD)"],"pagination":["1526-1542"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC6683004"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["18(8)"],"pubmed_abstract":["Systemin is a small peptide with important functions in plant wound response signaling. Although the transcriptional responses of systemin action are well described, the signaling cascades involved in systemin perception and signal transduction at the protein level are poorly understood. Here we used a tomato cell suspension culture system to profile phosphoproteomic responses induced by systemin and its inactive Thr17Ala analog, allowing us to reconstruct a systemin-specific kinase/phosphatase signaling network. Our time-course analysis revealed early phosphorylation events at the plasma membrane, such as dephosphorylation of H<sup>+</sup>-ATPase, rapid phosphorylation of NADPH-oxidase and Ca<sup>2+</sup>-ATPase. Later responses involved transient phosphorylation of small GTPases, vesicle"],"journal":["Molecular & cellular proteomics : MCP"],"pubmed_title":["The Systemin Signaling Cascade As Derived from Time Course Analyses of the Systemin-responsive Phosphoproteome."],"pmcid":["PMC6683004"],"funding_grant_id":["SFB1101/D06","1"],"pubmed_authors":["Wu XN","Stintzi A","Haj Ahmad F","Schaller A","Schulze WX"],"additional_accession":[]},"is_claimable":false,"name":"The Systemin Signaling Cascade As Derived from Time Course Analyses of the Systemin-responsive Phosphoproteome.","description":"Systemin is a small peptide with important functions in plant wound response signaling. Although the transcriptional responses of systemin action are well described, the signaling cascades involved in systemin perception and signal transduction at the protein level are poorly understood. Here we used a tomato cell suspension culture system to profile phosphoproteomic responses induced by systemin and its inactive Thr17Ala analog, allowing us to reconstruct a systemin-specific kinase/phosphatase signaling network. Our time-course analysis revealed early phosphorylation events at the plasma membrane, such as dephosphorylation of H<sup>+</sup>-ATPase, rapid phosphorylation of NADPH-oxidase and Ca<sup>2+</sup>-ATPase. Later responses involved transient phosphorylation of small GTPases, vesicle","dates":{"release":"2019-01-01T00:00:00Z","publication":"2019 Aug","modification":"2026-05-06T22:07:02.748Z","creation":"2025-05-31T22:25:25.751Z"},"accession":"S-EPMC6683004","cross_references":{"pubmed":["31138643"],"doi":["10.1074/mcp.RA119.001367"]}}