Krześlak Anna
Department of Cytobiochemistry, University of Lodz, 12/16 Banacha St., 90-237 Lódź, Poland.
Postepy Biochem. 2007;53(4):389-99.
Glycosylation, consisting in incorporation of single beta-N-acetyl-D-glucosamine residues attached by O-linkage to serine or threonine residues, is a common modification of cytoplasmic and nuclear proteins. Up to now about 200 proteins modified by O-GlcNAc have been identified including transcription factors, signaling components and metabolic enzymes. O-GlcNAc modified proteins can be also phosphorylated. In some cases O-GlcNAc and O-phosphate alternatively occupy the same sites. It has been suggested, that in signal transduction, instead of simple regulation by phosphorylation, more complex mechanism including glycosylation, is involved. Presented work focus on the structure and function of enzymes involved in O-GlcNAc modification and the role of this modification in regulating signal transduction and transcription.
糖基化是指单个β-N-乙酰-D-葡萄糖胺残基通过O-连接与丝氨酸或苏氨酸残基结合，是细胞质和细胞核蛋白常见的修饰方式。到目前为止，已鉴定出约200种被O-GlcNAc修饰的蛋白质，包括转录因子、信号转导成分和代谢酶。O-GlcNAc修饰的蛋白质也可以被磷酸化。在某些情况下，O-GlcNAc和O-磷酸会交替占据相同位点。有人提出，在信号转导中，涉及的是更复杂的机制，包括糖基化，而不是简单的磷酸化调节。目前的工作重点是参与O-GlcNAc修饰的酶的结构和功能，以及这种修饰在调节信号转导和转录中的作用。
