PARP1 promotes gene expression at the post-transcriptional level by modulating the RNA-binding protein HuR

Yueshuang Ke, Yanlong Han, Xiaolan Guo, Jitao Wen, Ke Wang, Xue Jiang, Xue Tian, Xueqing Ba (), Istvan Boldogh and Xianlu Zeng ()
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Yueshuang Ke: The Key Laboratory of Molecular Epigenetics of the Ministry of Education, Northeast Normal University
Yanlong Han: Institute of Genetics and Cytology, Northeast Normal University
Xiaolan Guo: Institute of Genetics and Cytology, Northeast Normal University
Jitao Wen: Institute of Genetics and Cytology, Northeast Normal University
Ke Wang: Institute of Genetics and Cytology, Northeast Normal University
Xue Jiang: Institute of Genetics and Cytology, Northeast Normal University
Xue Tian: Institute of Genetics and Cytology, Northeast Normal University
Xueqing Ba: The Key Laboratory of Molecular Epigenetics of the Ministry of Education, Northeast Normal University
Istvan Boldogh: Sealy Center for Molecular Medicine, University of Texas Medical Branch at Galveston
Xianlu Zeng: The Key Laboratory of Molecular Epigenetics of the Ministry of Education, Northeast Normal University

Nature Communications, 2017, vol. 8, issue 1, 1-16

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.

Date: 2017
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DOI: 10.1038/ncomms14632

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