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Mol Cell Proteomics. 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.

Author information

1
Program in Integrative Cell Signaling and Neurobiology of Metabolism and Section of Comparative Medicine, Department of Cellular & Molecular Physiology, Yale University School of Medicine, 333 Cedar Street, New Haven, Connecticut 06520;

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.

PMID:
23824911
PMCID:
PMC3861702
DOI:
10.1074/mcp.R113.029751
[Indexed for MEDLINE]
Free PMC Article

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