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- W2593505005 abstract "Abstract Poly(ADP-ribosyl)ation (PARylation) is mainly catalysed by poly-ADP-ribose polymerase 1 (PARP1), whose role in gene transcription modulation has been well established. Here we show that, in response to LPS exposure, PARP1 interacts with the adenylateuridylate-rich element-binding protein embryonic lethal abnormal vision-like 1 (Elavl1)/human antigen R (HuR), resulting in its PARylation, primarily at site D226. PARP inhibition and the D226 mutation impair HuR’s PARylation, nucleocytoplasmic shuttling and mRNA binding. Increases in mRNA level or stability of pro-inflammatory cytokines/chemokines are abolished by PARP1 ablation or inhibition, or blocked in D226A HuR-expressing cells. The present study demonstrates a mechanism to regulate gene expression at the post-transcriptional level, and suggests that blocking the interaction of PARP1 with HuR could be a strategy to treat inflammation-related diseases that involve increased mRNA stability." @default.
- W2593505005 created "2017-03-16" @default.
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- W2593505005 date "2017-03-08" @default.
- W2593505005 modified "2023-10-16" @default.
- W2593505005 title "PARP1 promotes gene expression at the post-transcriptional level by modulating the RNA-binding protein HuR" @default.
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- W2593505005 doi "https://doi.org/10.1038/ncomms14632" @default.
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- W2593505005 hasPublicationYear "2017" @default.
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