Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA, USA.
Department of Biochemistry and Molecular Biology, Drexel University College of Medicine, Philadelphia, PA, USA; Sidney Kimmel Cancer Center, Thomas Jefferson University, Philadelphia, PA, USA.
Cell Signal. 2022 Feb;90:110201. doi: 10.1016/j.cellsig.2021.110201. Epub 2021 Nov 17.
O-GlcNAcylation is a post-translational modification occurring on serine/threonine residues of nuclear and cytoplasmic proteins, mediated by the enzymes OGT and OGA which catalyze the addition or removal of the UDP-GlcNAc moieties, respectively. Structural changes brought by this modification lead to alternations of protein stability, protein-protein interactions, and phosphorylation. Importantly, O-GlcNAcylation is a nutrient sensor by coupling nutrient sensing with cellular signaling. Elevated levels of OGT and O-GlcNAc have been reported in a variety of cancers and has been linked to regulation of multiple cancer signaling pathways. In this review, we discuss the most recent findings on the role of O-GlcNAcylation as a metabolic sensor in signaling pathways and immune response in cancer.
O-GlcNAcylation 是一种发生在核蛋白和细胞质蛋白丝氨酸/苏氨酸残基上的翻译后修饰,由 OGT 和 OGA 这两种酶介导,它们分别催化 UDP-GlcNAc 部分的添加或去除。这种修饰带来的结构变化导致蛋白质稳定性、蛋白质-蛋白质相互作用和磷酸化的改变。重要的是,O-GlcNAcylation 通过将营养感应与细胞信号偶联,作为一种营养传感器。在各种癌症中已经报道了 OGT 和 O-GlcNAc 的水平升高,并与多种癌症信号通路的调节有关。在这篇综述中,我们讨论了 O-GlcNAcylation 作为代谢传感器在癌症信号通路和免疫反应中的最新发现。