Roles of protein ubiquitination in inflammatory bowel disease

Inflammatory bowel disease (IBD) including Crohn's disease (CD) and ulcerative colitis (UC) seriously affects the quality of life for patients. The pathogenesis of IBD contains the environmental, host genetic and epigenetic factors. In recent years, the studies of protein ubiquitination, an important protein post-translational modification as an epigenetic factor, have emerged in the pathogenesis and development of IBD. In the past few years, accumulative evidence illustrated that six E3 ubiquitin ligases, namely, ring finger protein (RNF) 183, RNF 20, A20, Pellino 3, TRIM62 and Itch, exhibited clear mechanisms in the development of IBD. They regulate the intestinal inflammation by facilitating the ubiquitination of targeted proteins which participate in different inflammatory signaling pathways. Besides, it was reported that some deubiquitinating enzymes such as Cylindromatosis and USP7 were involved in the development of IBD, but the molecular mechanism was still unclear. This review summarized the role and regulatory mechanism of protein ubiquitination in the pathogenesis and development of IBD, providing insights to develop a new therapeutic strategy in IBD treatments.