Developmentally regulated PERK activity renders dendritic cells insensitive to subtilase cytotoxin-induced integrated stress response
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Summary
It is shown that dendritic cells (DCs) display unusually high eIF2α phosphorylation, which is mostly caused by a developmentally regulated activation of the ER kinase PERK (EIF2AK3), and despite high p-eIF2 α levels, differentiated DCs display active protein synthesis and no signs of a chronic ISR.
- Type
- preprint
- Published
- 2020-04-28
- Cited by
- 0
- References
- 89
- Access
- Open access
- OpenAlex
- https://openalex.org/W3023411507
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:218489331
Keywords
Integrated stress response, ATF4, Cell biology, Phosphorylation, Biology
References
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- The small molecule ISRIB reverses the effects of eIF2α phosphorylation on translation and stress granule assembly
- MicroRNA-155 modulates the interleukin-1 signaling pathway in activated human monocyte-derived dendritic cells
- Stress‐induced gene expression requires programmed recovery from translational repression
- Regulation of translation is required for dendritic cell function and survival during activation
- Toll-like receptor activation suppresses endoplasmic reticulum stress-induced CHOP and translation inhibition through activation of eIF2B
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- Reprogramming mRNA translation during stress.
- Protein phosphatase 1 subunit Ppp1r15a/GADD34 regulates cytokine production in polyinosinic:polycytidylic acid-stimulated dendritic cells
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- Novel cross-talk within the IKK family controls innate immunity.
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