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Glycobiology and Extracellular Matrices
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- Cell BiologyOpen Access
TAILS N-terminomics and proteomics reveal complex regulation of proteolytic cleavage by O-glycosylation
Journal of Biological ChemistryVol. 293Issue 20p7629–7644Published online: March 28, 2018- Sarah L. King
- Christoffer K. Goth
- Ulrich Eckhard
- Hiren J. Joshi
- Amalie D. Haue
- Sergey Y. Vakhrushev
- and others
Cited in Scopus: 19Proteolytic 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.