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Integrative Proteomic Analysis of Posttranslational Modification in The Inflammatory Response

By Feiyang Ji, Menghao Zhou, Huihui Zhu, Zhengyi Jiang, Qirui Li, Xiaoxi Ouyang, Yiming Lv, Sainan Zhang, Tian Wu, Lanjuan Li

Posted 21 Jul 2020
bioRxiv DOI: 10.1101/2020.07.20.212134

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. ### Competing Interest Statement The authors have declared no competing interest.

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