O-GlcNAc modification:: a nutritional sensor that modulates proteasome function

被引:81
|
作者
Zachara, NE [1 ]
Hart, GW [1 ]
机构
[1] Johns Hopkins Univ, Sch Med, Dept Biol Chem, Baltimore, MD 21205 USA
关键词
D O I
10.1016/j.tcb.2004.03.005
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
The addition of O-linked beta-N-acetylglucosamine (O-GlcNAc) to serine and threonine residues is a post-translational modification of nucleocytoplasmic proteins that is thought to act in a manner analogous to protein phosphorylation. Recent work shows that many proteins of the metazoan proteasome are modified by O-GlcNAc and that the level of glycosylation is responsive to the nutritional state of the cell. Moreover, increased glycosylation of the 19S (or PA700) regulatory subcomplex has been correlated with decreased proteasomal activity, suggesting a new model of proteasomal regulation.
引用
收藏
页码:218 / 221
页数:4
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