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- W3120681821 endingPage "118953" @default.
- W3120681821 startingPage "118953" @default.
- W3120681821 abstract "Diacylglycerol kinase (DGK) constitutes a family of enzymes that phosphorylate diacylglycerol to phosphatidic acid (PA). These lipids serve as second messengers, thereby activating distinct downstream cascades and different cellular responses. Therefore, DG-to-PA conversion activity induces a phase transition of signaling pathways. One member of the family, DGKζ, is involved closely with stress responses. Morphological data showing that DGKζ localizes predominantly to the nucleus and that it shuttles between the nucleus and the cytoplasm implicate DGKζ in the regulation of transcription factors during stress responses. Tumor suppressor p53 and NF-κB are major stress-responsive transcription factors. They exert opposing effects on cellular pathophysiology. Herein, we summarize DGKζ catalytic activity-dependent and -independent regulatory mechanisms of p53 and NF-κB transactivation activities, including p53 degradation and NF-κB nuclear translocation. We also discuss how each component of DGKζ-interacting protein complex modulates the specificity and selectivity of target gene expression." @default.
- W3120681821 created "2021-01-18" @default.
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- W3120681821 creator A5044760409 @default.
- W3120681821 creator A5069303697 @default.
- W3120681821 date "2021-04-01" @default.
- W3120681821 modified "2023-09-26" @default.
- W3120681821 title "Regulation of p53 and NF-κB transactivation activities by DGKζ in catalytic activity-dependent and -independent manners" @default.
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- W3120681821 doi "https://doi.org/10.1016/j.bbamcr.2021.118953" @default.
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