Abstract:

Glycosylation and ubiquitination are two prevalent forms of post-translational modification（PTM） of proteins. They form a dynamic regulatory network through their interactions， jointly participating in the regulation of key biological processes such as maintenance of protein homeostasis， signal transduction cascades， and cellular differentiation and development. Glycosylation can influence the ubiquitination process by regulating the activity and substrate specificity of ubiquitin ligase. Conversely， ubiquitination can reciprocally regulate the occurrence and types of glycosylation by altering the stability of glycosyltransferases and the spatial conformation of their substrates. Current evidence indicates that the dysregulation of the dynamic balance of these two modifications and the disruption of their regulatory network are closely associated with pathological processes such as tumorigenesis and progression， viral immune evasion， and metabolic syndrome. Based on recent domestic and international literature， this article summarized the biological functions of glycosylation and ubiquitination modifications， as well as their mutual regulatory roles in the development and progression of diseases including tumor and viral infection. The feasibility of targeting key molecules involved in the glycosylation and ubiquitination processes as potential therapeutic targets was also discussed， aiming to provide theoretical support for the treatment strategies of tumor and viral infection.

Key words: Glycosylation, Ubiquitination, Deubiquitinating enzyme, Tumor, Virus