TAILS N-terminomics and proteomics reveal complex regulation of proteolytic cleavage by O-glycosylation.

ABSTRACT: Proteolytic processing is an irreversible post-translational modification functioning as a ubiquitous regulator of cellular activity. Protease activity is tightly regulated via control of gene expression, enzyme and substrate compartmentalization, zymogen activation, enzyme inactivation, and substrate availability. Emerging evidence suggests that proteolysis can also be regulated by substrate glycosylation and that glycosylation of individual sites on a substrate can decrease or, in rare cases, increase its sensitivity to proteolysis. Here, we investigated the relationship between site-specific, mucin-type (or GalNAc-type) O-glycosylation and proteolytic cleavage of extracellular proteins. Using in silico analysis, we found that O-glycosylation and cleavage sites are s

SUBMITTER: King SL 

PROVIDER: S-EPMC5961060 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature