期刊
NATURE COMMUNICATIONS
卷 9, 期 -, 页码 -出版社
NATURE PUBLISHING GROUP
DOI: 10.1038/s41467-018-03417-3
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资金
- European Community [283570]
- German Research Foundation (Emmy Noether Program) [BE 5342/1-1, SFB 1177]
- Marie Curie Career Integration Grant from the European Commission [630763]
- LOEWE program Ubiquitin Networks (Ub-Net) of the State of Hesse (Germany)
- Else Kroner-Fresenius-Stiftung [2015_A124]
- Else Kroner-Forschungskolleg Frankfurt
- Leibniz Award
- Cluster of Excellence Macromolecular Complexes [EXC115]
- Volkswagen Stiftung
- Novo Nordisk Foundation [NNF14CC0001]
- Lundbeck Foundation [R190-2014-4037] Funding Source: researchfish
- Novo Nordisk Foundation Center for Protein Research [PI Chunaram Choudhary, PI Niels Mailand] Funding Source: researchfish
Ultraviolet (UV) light radiation induces the formation of bulky photoproducts in the DNA that globally affect transcription and splicing. However, the signaling pathways and mechanisms that link UV-light-induced DNA damage to changes in RNA metabolism remain poorly understood. Here we employ quantitative phosphoproteomics and protein kinase inhibition to provide a systems view on protein phosphorylation patterns induced by UV light and uncover the dependencies of phosphorylation events on the canonical DNA damage signaling by ATM/ATR and the p38 MAP kinase pathway. We identify RNA-binding proteins as primary substrates and 14-3-3 as direct readers of p38-MK2-dependent phosphorylation induced by UV light. Mechanistically, we show that MK2 phosphorylates the RNA-binding subunit of the NELF complex NELFE on Serine 115. NELFE phosphorylation promotes the recruitment of 14-3-3 and rapid dissociation of the NELF complex from chromatin, which is accompanied by RNA polymerase II elongation.
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