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. 2018 Mar 9;9:1017. doi: 10.1038/s41467-018-03417-3

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© The Author(s) 2018

Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/.

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Fig. 2 — MK2/3 are key transducers of p38 signaling after UV light. a Schematic representation of the strategy used to identify UV-light-induced, MK2/3/5-dependent phosphorylation sites. SILAC-labeled U2OS cells were mock-treated (Light), pretreated with the p38 inhibitor (Medium) or the MK2/3/5 inhibitor (Heavy), and subsequently irradiated with UV light (40 J/m², 1 h recovery). The phosphoproteome analysis was performed as described in Fig. 1c. b The scatter plot shows the logarithmized SILAC ratios of quantified phosphorylation sites. The color-coding indicates the density. A majority of UV-light-induced, p38-dependent phosphorylation sites significantly decreased in abundance also after MK2/3/5 inhibition, whereas a smaller fraction of sites decreased in abundance only after p38 inhibition. c The bar graph shows the percentage of UV-light-upregulated, p38-dependent sites that are up-, non-, or downregulated after MK2/3/5 inhibition. Nearly 60% of p38-dependent phosphorylation sites are also dependent on MK2/3/5. d Sequence motif analysis of p38- and MK2/3/5-dependent phosphorylation sites. The analysis was done as described in Fig. 1e. The sequence surrounding the phosphorylated residue shows an enrichment of glutamine (Q) in position – 2, arginine (R) in – 3, and leucine (L) in – 5. e Sequence motif analysis of p38-dependent, MK2/3/5-independent sites phosphorylation sites. The analysis was done as described in Fig. 1e. The sequence surrounding the phosphorylated residue shows an enrichment of aspartic acid (D) in position + 2, + 4, and arginine (R) in – 3. f The scatter plot shows the logarithmized SILAC ratios of quantified proteins. 14-3-3 interaction partners and p38-dependent interactions are indicated in light and dark red, respectively. Three hundred and eighty-four proteins were significantly enriched in 14-3-3 pull downs after UV light (p-value < 0.05, moderated t-test). One hundred and eight out of 384 proteins (28%) bound to 14-3-3 in a p38-dependent manner. g The bar plot shows the number of proteins with the indicated Gene Ontology (GO)-molecular function terms that were enriched among p38-dependent 14-3-3 interaction partners. h The table shows selected RNA-binding proteins that were identified as p38-dependent interaction partners of 14-3-3. The UniProt ID, protein name, gene name, position(s), and sequence window of UV-light-induced phosphorylation sites identified in phosphoproteomics screen is indicated