biostudies-literatureCampbell AECancer Research UKBiotechnology and Biological Sciences Research Council533-551https://www.ebi.ac.uk/biostudies/studies/S-EPMC7886319biostudies-literatureUnknown478(3)Different types of DNA damage can initiate phosphorylation-mediated signalling cascades that result in stimulus specific pro- or anti-apoptotic cellular responses. Amongst its many roles, the NF-κB transcription factor RelA is central to these DNA damage response pathways. However, we still lack understanding of the co-ordinated signalling mechanisms that permit different DNA damaging agents to induce distinct cellular outcomes through RelA. Here, we use label-free quantitative phosphoproteomics to examine the temporal effects of exposure of U2OS cells to either etoposide (ETO) or hydroxyurea (HU) by monitoring the phosphorylation status of RelA and its protein binding partners. Although few stimulus-specific differences were identified in the constituents of phosphorylated RelA interactomThe Biochemical journalTemporal modulation of the NF-κB RelA network in response to different types of DNA damage.PMC7886319C1443/A12750BB/R000182/122095BB/L009501/1BB/M012557/1BB/L006480/1C1443/A22095Perkins SCorbin EKCampbell AEFerraz Franco CPerkins NDKalyuzhnyy AEyers CEJones ARSu LIBrownridge PJfalseTemporal modulation of the NF-κB RelA network in response to different types of DNA damage.Different types of DNA damage can initiate phosphorylation-mediated signalling cascades that result in stimulus specific pro- or anti-apoptotic cellular responses. Amongst its many roles, the NF-κB transcription factor RelA is central to these DNA damage response pathways. However, we still lack understanding of the co-ordinated signalling mechanisms that permit different DNA damaging agents to induce distinct cellular outcomes through RelA. Here, we use label-free quantitative phosphoproteomics to examine the temporal effects of exposure of U2OS cells to either etoposide (ETO) or hydroxyurea (HU) by monitoring the phosphorylation status of RelA and its protein binding partners. Although few stimulus-specific differences were identified in the constituents of phosphorylated RelA interactom2021-01-01T00:00:00Z2021 Feb2026-04-30T17:08:09.736Z2021-02-26T08:18:52ZS-EPMC78863193343874610.1042/BCJ20200627