蛋白质O-GlcNAc糖基化及其细胞生物学功能  

Protein O-GlcNAc Modification and Its Cytobiology Function

作　　者：杨新颖[1] 李静[1] 耿美玉[1] 

机构地区：[1]中国海洋大学医药学院分子药理室,青岛266003

出　　处：《细胞生物学杂志》2007年第5期682-686,共5页Chinese Journal of Cell Biology

基　　金：国家重点基础研究发展规划(973计划)(No.2003CB716400)资助项目~~

摘　　要：糖基化是蛋白质翻译后修饰的一项重要内容,大多数蛋白质糖基化发生在细胞膜表面,且糖链结构复杂。而发生在细胞浆与细胞核内的、单个O-GlcNAc修饰的蛋白质糖基化现象,因其独特的细胞定位、糖链连接方式以及重要的生物学调控作用而日益成为糖生物学领域研究的热点。现对蛋白质O-GlcNAc修饰及其细胞生物学功能研究进展情况进行综述。Glycosylation is one of the most important contents of protein posttranslational modification. Most of protein glycosylations take place at cells membrane and the glycan structure is complex. Another form of protein glycosylation, O-^-N-acetylglucosamine （O-GlcNAc）, existing extensively in nuclear and cytosolic proteins was observed recently, which will become the hotspot in glycobiology study increasingly for its special cell location and linkage style and the important role in cellular regulation. The unique carbohydrate modification O-GlcNAc and its application in cell biology was reviewed.

关 键 词：O-GLCNAC O-磷酸化 OGT O-GLCNACASE 阴-阳学说 

分 类 号：Q26[生物学—细胞生物学]