Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes

  title={Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes},
  author={David James Gill and Joanne Chia and Jamie Senewiratne and Frederic Bard},
  booktitle={The Journal of cell biology},
After growth factor stimulation, kinases are activated to regulate multiple aspects of cell physiology. Activated Src is present on Golgi membranes, but its function here remains unclear. We find that Src regulates mucin-type protein O-glycosylation through redistribution of the initiating enzymes, polypeptide N-acetylgalactosaminyl transferases (GalNac-Ts), from the Golgi to the ER. Redistribution occurs after stimulation with EGF or PDGF in a Src-dependent manner and in cells with… CONTINUE READING

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Publications referenced by this paper.
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High density O - glycosylation on tandem repeat peptide from secretory MUC 1 of T 47 D breast cancer cells

S. Müller, K. Alving, +3 authors F. G. Hanisch
J . Biol . Chem . • 1999
View 1 Excerpt
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