Proteomics

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Regulation of the stress proteome 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 prevents cytotoxic stress but the mechanisms are diffuse. We investigated changes in the proteome of NIH-3T3 fibroblasts upon induction of cytotoxic stress (valinomycin or myrtucommulone A) and SCD1 inhibition (CAY10566) and addressed the potential of PI(18:1/18:1) and PI(16:0/16:0) to compensate for the decrease in SCD1 activity.

INSTRUMENT(S): Orbitrap Fusion

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Culture, Fibroblast

SUBMITTER: Konstantin Neukirch  

LAB HEAD: Andreas Koeberle

PROVIDER: PXD025396 | Pride | 2022-04-06

REPOSITORIES: Pride

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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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