Work

Regulation of Protein Degradation by O-GlcNAcylation: Crosstalk with Ubiquitination

Year: 2013

Type: review

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.

Source: Molecular & Cellular Proteomics

DOI: 10.1074/mcp.r113.029751

Authors: Hai-Bin Ruan, Yongzhan Nie, Xiaoyong Yang

Institutions: Yale University, Xijing Hospital, State Key Laboratory of Cancer Biology, Air Force Medical University

Language: English

Topic: Glycosylation and Glycoproteins Research

Subfield: Molecular Biology

Field: Biochemistry, Genetics and Molecular Biology

Domain: Life Sciences

SDG: Good health and well-being

Open Access status: hybrid

Estimated APC paid: $3,430