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Review
. 2013 Dec;12(12):3489-97.
doi: 10.1074/mcp.R113.029751. Epub 2013 Jul 3.

Regulation of protein degradation by O-GlcNAcylation: crosstalk with ubiquitination

Hai-Bin Ruan  1 , Yongzhan Nie, Xiaoyong Yang
Affiliations
Review

Regulation of protein degradation by O-GlcNAcylation: crosstalk with ubiquitination

Hai-Bin Ruan et al. Mol Cell Proteomics. 2013 Dec.

Abstract

The post-translational modification of intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) regulates essential cellular processes such as signal transduction, transcription, translation, and protein degradation. Misfolded, damaged, and unwanted proteins are tagged with a chain of ubiquitin moieties for degradation by the proteasome, which is critical for cellular homeostasis. In this review, we summarize the current knowledge of the interplay between O-GlcNAcylation and ubiquitination in the control of protein degradation. Understanding the mechanisms of action of O-GlcNAcylation in the ubiquitin-proteosome system shall facilitate the development of therapeutics for human diseases such as cancer, metabolic syndrome, and neurodegenerative diseases.

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Figures

Fig. 1.
Fig. 1.
Modes of interaction between O-GlcNAcylation and ubiquitination. A, O-GlcNAcylation of the substrate antagonizes phosphorylation at the same or adjacent site to control ubiquitination. B, O-GlcNAcylation provides a docking site for DUBs that deubiquitinate the substrate. C, O-GlcNAcylation of H2B recruits an E3 complex to monoubiquitinate H2B. D, targeting the ubiquitin-proteasome system. OGT physically interacts with ubiquitin precursors, E3s, and DUBs. O-GlcNAcylation has been found on E1s, E3s, DUBs, and 19S and 20S proteasomes.
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