摘要
Posttranslational modifications(PTMs)of proteins,particularly acetylation,phosphorylation,and ubiquitination,play critical roles 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.
基金
supported by the National Key R&D Program of China(Grant Nos.2016YFC1101304/3 and 2017YFC1200100)
the National Natural Science Foundation of China(Grant No.81400589)
the National S&T Major Project,China(Grant No.2017ZX10202202-001-008)
the Science Fund for Creative Research Groups of the National Natural Science Foundation,China(Grant No.81721091)。
