Link to bioRxiv paper: http://biorxiv.org/cgi/content/short/2020.07.20.212134v1?rss=1 Authors: Ji, F., Zhou, M., Zhu, H., Jiang, Z., Li, Q., Ouyang, X., Lv, Y., Zhang, S., Wu, T., Li, L. Abstract: The posttranslational modification (PTM) of proteins, particularly acetylation, phosphorylation and ubiquitination, plays a critical role in the host innate immune response. PTMs dynamic changes and the crosstalk among them are complicated. To build a comprehensive dynamic network of inflammation related proteins, we integrated data from the whole cell proteome (WCP), acetylome, phosphoproteome and ubiquitinome of human and mouse macrophages. Our datasets of acetylation, phosphorylation and ubiquitination sites helped identify PTM crosstalk within and across proteins involved in the inflammatory response. Stimulation of macrophages by lipopolysaccharide (LPS) resulted in both degradative and non-degradative ubiquitination. Moreover, this study contributes to the interpretation of the roles of known inflammatory molecules and the discovery of novel inflammatory proteins. Copy rights belong to original authors. Visit the link for more info