AI Article Synopsis
- O-GlcNAcylation, a post-translational modification where a single N-acetylglucosamine sugar is added to proteins, plays a crucial yet often overlooked role in apoptosis.
- This modification is dynamic and reversible, sharing similarities with phosphorylation rather than traditional glycosylation methods.
- The review highlights how GlcNAcylation, influenced by O-GlcNAc transferase (OGT) and bacterial proteins, modulates the extrinsic apoptotic pathway and affects cell fate decisions.
Article Abstract
The importance of post-translational modifications (PTMs), particularly O-GlcNAcylation, of cytoplasmic proteins in apoptosis has been neglected for quite a while. Modification of cytoplasmic proteins by a single N-acetylglucosamine sugar is a dynamic and reversible PTM exhibiting properties more like phosphorylation than classical O- and N-linked glycosylation. Due to the sparse information existing, we have only limited understanding of how GlcNAcylation affects cell death. Deciphering the role of GlcNAcylation in cell fate may provide further understanding of cell fate decisions. This review focus on the modulation of extrinsic apoptotic pathway via GlcNAcylation carried out by O-GlcNAc transferase (OGT) or by other bacterial effector proteins.
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| http://dx.doi.org/10.1016/j.tcb.2024.01.003 | DOI Listing |
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