Journal
TRENDS IN CELL BIOLOGY
Volume 21, Issue 3, Pages 149-158Publisher
ELSEVIER SCIENCE LONDON
DOI: 10.1016/j.tcb.2010.11.004
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Funding
- A*Star funds
- Carlsberg Foundation
- Danish Research Councils
- University of Copenhagen
- EMBO long-term fellowship
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O-GaINAc 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 GaINAc-transferases (GaINAc-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 GaINAc-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 GaINAc-Ts could play an important role in cancerous cellular transformation.
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