AI Article Synopsis
- - O-linked-N-acetylglucosaminylation (O-GlcNAcylation) is a vital modification in proteins that affects their stability, functionality, and interactions by attaching a sugar molecule to specific amino acids (serine and threonine).
- - O-linked N-acetylglucosamine transferase (OGT) is the enzyme that facilitates this modification, and its overexpression is linked to various cancers, influencing tumor growth, metabolism, and resistance to drugs.
- - The review discusses how OGT operates biochemically in tumors and suggests that targeting this enzyme may offer new strategies for cancer treatment.
Article Abstract
O-linked-N-acetylglucosaminylation (O-GlcNAcylation) is a common and important post-translational modification (PTM) linking O-linked β-N-acetylglucosamine (O-GlcNAc) to serine and threonine residues in proteins. Extensive research indicates its impact on target protein stability, activity, and interactions. O-linked N-acetylglucosamine transferase (OGT) is a critical enzyme that catalyzes O-GlcNAc modification, responsible for adding O-GlcNAc to proteins. OGT and O-GlcNAcylation are overexpressed in many tumors and closely associated with tumor growth, invasion, metabolism, drug resistance, and immune evasion. This review delineates the biochemical functions of OGT and summarizes its effects and mechanisms in tumors. Targeting OGT presents a promising novel approach for treating human malignancies.
Download full-text PDF |
Source |
|---|---|
| http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11406787 | PMC |
| http://dx.doi.org/10.1186/s13578-024-01301-w | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Want AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!