Modulation of transcription factor function by O-GlcNAc modification.
Modulation of transcription factor function by O-GlcNAc modification.
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通过O-GLCNAC修饰调节转录因子功能。
DOI：
10.1016/j.bbagrm.2010.02.005
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发表时间：
2010-05
影响因子：
4.7
通讯作者：
Cantrell, Jamie E. L.
中科院分区：
文献类型：
--
作者：
Ozcan, Sabire;Andrali, Sreenath S.;Cantrell, Jamie E. L.
细胞核和细胞质蛋白的O-连接β-N-乙酰葡糖胺（O-GlcNAc）修饰对于许多细胞过程很重要，含有这种修饰的蛋白质数量正在稳步增加。这种修饰是动态和可逆的，并且在某些情况下竞争相同残基的磷酸化。蛋白质的O-GlcNAc修饰受细胞周期、营养代谢和其他细胞外信号调节。与由大量激酶介导的蛋白质磷酸化相比，O-GlcNAc修饰仅由一种称为O-连接的N-乙酰葡糖胺基转移酶或OGT的酶催化。从蛋白质中去除O-GlcNAc由β-N-乙酰氨基葡糖苷酶（O-GlcNAc酶或OGA）催化。改变的O-连接GlcNAc修饰水平有助于许多疾病的建立，例如癌症、糖尿病、心血管疾病和神经变性。许多转录因子已被证明是由O-连接的GlcNAc修饰，这可以影响它们的转录活性，DNA结合，定位，稳定性和与其他辅因子的相互作用。本文综述了O-连接的GlcNAc修饰对转录因子功能的调节作用。
O-linked beta-N-acetylglucosamine (O-GlcNAc) modification of nuclear and cytoplasmic proteins is important for many cellular processes, and the number of proteins that contain this modification is steadily increasing. This modification is dynamic and reversible, and in some cases competes for phosphorylation of the same residues. O-GlcNAc modification of proteins is regulated by cell cycle, nutrient metabolism, and other extracellular signals. Compared to protein phosphorylation, which is mediated by a large number of kinases, O-GlcNAc modification is catalyzed only by one enzyme called O-linked N-acetylglucosaminyl transferase or OGT. Removal of O-GlcNAc from proteins is catalyzed by the enzyme beta-N-acetylglucosaminidase (O-GlcNAcase or OGA). Altered O-linked GlcNAc modification levels contribute to the establishment of many diseases, such as cancer, diabetes, cardiovascular disease, and neurodegeneration. Many transcription factors have been shown to be modified by O-linked GlcNAc modification, which can influence their transcriptional activity, DNA binding, localization, stability, and interaction with other co-factors. This review focuses on modulation of transcription factor function by O-linked GlcNAc modification.
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