Lead Editor:
Professor Lydia Meder,
Friedrich-Alexander-Universität Erlangen-Nürnberg,
Germany
Glycosylation, a prevalent post-translational modification of proteins, comprises two principal types: O-glycosylation and N-glycosylation. O-glycosylation involves the attachment of carbohydrates to serine and threonine residues of proteins, significantly influencing protein function, stability, and localization. In cancer, aberrantly O-glycosylated proteins serve as markers of poor prognosis, drivers of tumorigenesis, and mediators of therapy resistances. These altered cancer-associated O-glycosylations are frequently caused by aberrations in the activity of glycosyltransferases, which catalyze the transfer of carbohydrates to glycoproteins and glycolipids. Changes in the glycan structure, comprising also abnormal fucosylation and sialyation, affect protein-protein interactions contributing to cancer progression and metastasis. Unravelling O-glycosylation-dependent mechanisms in the tumor microenvironment will be important to understand processes in cancer and therapy resistance and to identify new biomarkers. This special issue will focus on cancer-related changes in O-glycosylation covering: mechanisms driven by glycosyltransferases, effects in the tumor microenvironment and the functional links to metastasis and therapy resistance.
Submission deadline:
11/07/2026
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