Proteomics

Dataset Information

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Regulation of stress signaling by SCD1


ABSTRACT: Cytotoxic stress activates stress-activated kinases, initiates adaptive mechanisms, including the unfolded protein response (UPR) and autophagy, and induces programmed cell death. Fatty acid unsaturation, controlled by stearoyl-CoA desaturase (SCD)1, prevents cytotoxic stress but the mechanisms are diffuse. We found that SCD1 inhibition alters the levels of proteins phosphorylated at tyrosine in fibroblasts. Major regulated proteins were identified following immunoprecipitation using an anti-phospho-tyrosine antibody and subsequent proteomic analysis.

INSTRUMENT(S): Synapt MS

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Culture, Fibroblast

SUBMITTER: Andreas Koeberle  

LAB HEAD: Andreas Koeberle

PROVIDER: PXD031890 | Pride | 2022-03-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
181122_band_1_CAY.xml Xml
181122_band_1_CAY.zip Other
181122_band_1_CAY_isotype_control.xml Xml
181122_band_1_CAY_isotype_control.zip Other
181122_band_1_w-o.xml Xml
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Publications


Cytotoxic stress activates stress-activated kinases, initiates adaptive mechanisms, including the unfolded protein response (UPR) and autophagy, and induces programmed cell death. Fatty acid unsaturation, controlled by stearoyl-CoA desaturase (SCD)1, prevents cytotoxic stress but the mechanisms are diffuse. Here, we show that 1,2-dioleoyl-sn-glycero-3-phospho-(1'-myo-inositol) [PI(18:1/18:1)] is a SCD1-derived signaling lipid, which inhibits p38 mitogen-activated protein kinase activation, count  ...[more]

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