Dataset Information

Perception of the peptide hormone Systemin

ABSTRACT: Cell suspension cultures of Solanum peruvianum were subjected to stimulation with 10nM systemin, the inactive systemin analog10nM a17, or injected with equal volume of water. For each treatment, a batch of cells was harvested after 2 minutes, 5 minutes, 15 minutes and 45 minutes. Untreated cells were harvested as controls. All treatments and time points were sampled as three independent replicates using independent sets of cells. Microsomal membranes were isolated from each sample, digested with trypsin, enriched for phosphopeptides and subjected to untargeted data-dependent acquisition by LC-MS/MS. Data analysis was performed jointly for all samples, and intensity values of triplicates were averaged.

INSTRUMENT(S): Q Exactive

ORGANISM(S): Solanum Peruvianum

TISSUE(S): Plant Cell, Cell Suspension Culture

DISEASE(S): Disease Free

SUBMITTER: Fatima Haj Ahmad

LAB HEAD: Andreas Klaus Schaller

PROVIDER: PXD010819 | Pride | 2019-06-17

REPOSITORIES: Pride

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Publications

The Systemin Signaling Cascade As Derived from Time Course Analyses of the Systemin-responsive Phosphoproteome.

Haj Ahmad Fatima F Wu Xu Na XN Stintzi Annick A Schaller Andreas A Schulze Waltraud X WX

Molecular & cellular proteomics : MCP 20190528 8

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 ...[more]

PMID: 31138643

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Project description:Poly(ADP-ribose) Polymerase 1 (PARP-1) is a nuclear enzyme that catalyse the transfer of ADP-ribose units from NAD+ to several target proteins involved in cellular stress responses. Using the cell line WRL68, we have previously shown that the activation of PARP-1 induced by oxidative stress after H2O2 treatment lead to depletion of cellular NAD+ and ATP, which promote cell death. In this work, we used LC-MS/MS based phosphoproteomics to show that the oxidative damage induced by H2O2 treatment modified the phosphorylation of several proteins in WRL68 cells, most of them related to transcription process. Interestingly, genetic or pharmacological inhibition of PARP-1 reduced the phosphorylation of YAP1, a transcriptional coactivator involved in cell survival, in WRL68 cells after H2O2 treatment. Inhibition of PARP-1 increased cell viability after oxidative treatment and diminished the degradation of YAP1; the elimination of YAP1 by gene silencing abrogated the protective effect of PARP-1 inhibition, indicating that YAP1 is important for the survival of WRL68 cells after oxidative damage. In the same way, the supplementation of NAD+, substrate of PARP-1, on WRL68 cells suffering oxidative damage reduced the phosphorylation of YAP1, suggesting that the loss of cellular NAD+ caused by PARP-1 activation after oxidative treatment is responsible for the phosphorylation of YAP1. Finally, PARP-1 silencing after oxidative treatment diminished the activation of AMPK, a master regulator of cell metabolism implicated in the restoration of energy balance during metabolic stress. Since NAD+ supplementation reduced the phosphorylation of some AMPK substrates in WRL68 cells after oxidative treatment, we hypothesize that the loss of cellular NAD+ after PARP-1 activation may induce a metabolic stress that activates AMPK. In summary, we showed a new crucial role of PARP-1 in the response to oxidative stress in WRL68 cells; PARP-1 activation reduces the cell viability by promoting the phosphorylation and degradation of YAP1, which is mediated by the energy stress caused by PARP-1 activation.

Dataset Information

Perception of the peptide hormone Systemin

Publications

The Systemin Signaling Cascade As Derived from Time Course Analyses of the Systemin-responsive Phosphoproteome.

Similar Datasets

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