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

Hai Bin Ruan, Yongzhan Nie, Xiaoyong Yang

Research output: Contribution to journalReview articlepeer-review

78 Scopus citations

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.

Original languageEnglish (US)
Pages (from-to)3489-3497
Number of pages9
JournalMolecular and Cellular Proteomics
Volume12
Issue number12
DOIs
StatePublished - Dec 2013

Fingerprint Dive into the research topics of 'Regulation of protein degradation by O-GlcNAcylation: Crosstalk with ubiquitination'. Together they form a unique fingerprint.

Cite this