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.

细胞质蛋白的翻译后修饰 (PTM)，特别是 O-GlcNAc 修饰在细胞凋亡中的重要性长期以来一直被忽视。单个 N-乙酰氨基葡萄糖对细胞质蛋白的修饰是一种动态且可逆的 PTM，其表现出的特性更像是磷酸化，而不是经典的 O- 和 N- 连接糖基化。由于现有信息稀疏，我们对 GlcNAcylation 如何影响细胞死亡的了解有限。破译 GlcNAc 酰化在细胞命运中的作用可能有助于进一步了解细胞命运的决定。本综述重点关注通过 O-GlcNAc 转移酶 (OGT) 或其他细菌效应蛋白进行的 GlcNAc 酰化来调节外源性细胞凋亡途径。