丝氨酸
磷酸化
苏氨酸
串扰
细胞生物学
免疫系统
生物
信号转导
糖基化
激酶
转移酶
生物化学
细胞质
酶
遗传学
物理
光学
作者
Yi-Hsuan Chang,Chia-Lin Weng,Kuo‐I Lin
标识
DOI:10.1186/s12929-020-00648-9
摘要
Abstract O -linked-N-acetylglucosaminylation ( O -GlcNAcylation) is a type of glycosylation that occurs when a monosaccharide, O -GlcNAc, is added onto serine or threonine residues of nuclear or cytoplasmic proteins by O -GlcNAc transferase (OGT) and which can be reversibly removed by O -GlcNAcase (OGA). O -GlcNAcylation couples the processes of nutrient sensing, metabolism, signal transduction and transcription, and plays important roles in development, normal physiology and physiopathology. Cumulative studies have indicated that O -GlcNAcylation affects the functions of protein substrates in a number of ways, including protein cellular localization, protein stability and protein/protein interaction. Particularly, O -GlcNAcylation has been shown to have intricate crosstalk with phosphorylation as they both modify serine or threonine residues. Aberrant O -GlcNAcylation on various protein substrates has been implicated in many diseases, including neurodegenerative diseases, diabetes and cancers. However, the role of protein O -GlcNAcylation in immune cell lineages has been less explored. This review summarizes the current understanding of the fundamental biochemistry of O -GlcNAcylation, and discusses the molecular mechanisms by which O -GlcNAcylation regulates the development, maturation and functions of immune cells. In brief, O -GlcNAcylation promotes the development, proliferation, and activation of T and B cells. O -GlcNAcylation regulates inflammatory and antiviral responses of macrophages. O -GlcNAcylation promotes the function of activated neutrophils, but inhibits the activity of nature killer cells.
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