Abstract
O-GalNAc glycosylation of proteins confers essential structural, protective and signaling roles in eumetazoans. Addition of O-glycans onto proteins is an extremely complex process that regulates both sites of attachment and the types of oligosaccharides added. Twenty distinct polypeptide GalNAc-transferases (GalNAc-Ts) initiate O-glycosylation and fine-tuning their expression provides a mechanism for regulating this action. Recently, a new mode of regulation has emerged where activation of Src kinase selectively redistributes Golgi-localized GalNAc-Ts to the ER. This relocalization results in a strong increase in the density of O-glycan decoration. In this review, we discuss how different mechanisms can regulate the number and the types of O-glycans decorating proteins. In addition, we speculate how Src-dependent relocation of GalNAc-Ts could play an important role in cancerous cellular transformation.
| Original language | English |
|---|---|
| Journal | Trends in Cell Biology |
| Volume | 21 |
| Issue number | 3 |
| Pages (from-to) | 149-58 |
| Number of pages | 10 |
| ISSN | 0962-8924 |
| DOIs | |
| Publication status | Published - 1 Mar 2011 |
Keywords
- Animals
- Glycoproteins
- Glycosylation
- Humans
- N-Acetylgalactosaminyltransferases
- Polysaccharides
- Protein Transport
- Substrate Specificity
