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. © 2013 by The American Society for Biochemistry and Molecular Biology, Inc.
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CITATION STYLE
Ruan, H. B., Nie, Y., & Yang, X. (2013, December). Regulation of protein degradation by O-GlcNAcylation: Crosstalk with ubiquitination. Molecular and Cellular Proteomics. https://doi.org/10.1074/mcp.R113.029751
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