4.6

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2.2

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  • ISSN 1674-8301
  • CN 32-1810/R
Meryem Bektas, David S. Rubenstein. The role of intracellular protein O-glycosylation in cell adhesion and disease[J]. The Journal of Biomedical Research, 2011, 25(4): 227-236. DOI: 10.1016/S1674-8301(11)60031-6
Citation: Meryem Bektas, David S. Rubenstein. The role of intracellular protein O-glycosylation in cell adhesion and disease[J]. The Journal of Biomedical Research, 2011, 25(4): 227-236. DOI: 10.1016/S1674-8301(11)60031-6

The role of intracellular protein O-glycosylation in cell adhesion and disease

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This work was supported by NIH RO1 (No. AI49427) to Dr David S. Rubenstein.

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  • Post-translational protein modification, including phosphorylation, is generally quick and reversible, facilitat-ing rapid biologic adjustments to altered cellular physiologic demands. In addition to protein phosphorylation, other post-translational modifications have been identified. Intracellular protein O-glycosylation, the addition of the simple sugar O-linked N-acetylglucosamine (O-GlcNAc) to serine/threonine residues, is a relatively recently identified post-translational modification that has added to the complexity by which protein function is regulated. Two intracellular enzymes, O-GlcNAc transferase and O-GlcNAcase, catalyze the addition and removal, respec-tively, of O-GlcNAc to serine and threonine side-chain hydroxyl groups. Numerous proteins, including enzymes, transcription factors, receptors and structural proteins have been shown to be modified by intracellular O-glyco-sylation. In this review, the mechanism and relevance of O-GlcNAc protein modification are discussed in the con-text of cell adhesion and several representative diseases.
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