Please use this identifier to cite or link to this item: https://doi.org/10.1083/jcb.201003055
Title: Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes
Authors: Gill, D.J.
Chia, J.
Senewiratne, J.
Bard, F. 
Issue Date: 31-May-2010
Citation: Gill, D.J., Chia, J., Senewiratne, J., Bard, F. (2010-05-31). Regulation of O-glycosylation through Golgi-to-ER relocation of initiation enzymes. Journal of Cell Biology 189 (5) : 843-858. ScholarBank@NUS Repository. https://doi.org/10.1083/jcb.201003055
Abstract: 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 constitutively elevated Src activity. All GalNac-T family enzymes tested are affected, whereas multiple other glycosylation enzymes are not displaced from the Golgi. Upon Src activation, the COP-I coat is also redistributed in punctate structures that colocalize with GalNac-Ts and a dominant-negative Arf1 isoform, Arf1(Q71L), efficiently blocks GalNac-T redistribution, indicating that Src activates a COP-I-dependent trafficking event. Finally, Src activation increases O-glycosylation initiation as seen by lectin staining and metabolic labeling. We propose that growth factor stimulation regulates O-glycosylation initiation in a Src-dependent fashion by GalNac-T redistribution to the ER. © 2010 Gill et al.
Source Title: Journal of Cell Biology
URI: http://scholarbank.nus.edu.sg/handle/10635/125338
ISSN: 00219525
DOI: 10.1083/jcb.201003055
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