THE PHOSPHORYLATION OF STATHMIN BY MAP KINASE

被引：66

作者：

LEIGHTON, IA ^{[1
]}

CURMI, P ^{[1
]}

CAMPBELL, DG ^{[1
]}

COHEN, P ^{[1
]}

SOBEL, A ^{[1
]}

机构：

[1] CNRS,URA 614,INSERM,U153,F-75005 PARIS,FRANCE

来源：

MOLECULAR AND CELLULAR BIOCHEMISTRY | 1993年 / 128卷

关键词：

MAP KINASE; PC12; CELLS; NERVE GROWTH FACTOR; STATHMIN; PROTEIN KINASE;

D O I：

10.1007/BF01076766

中图分类号：

Q2 [细胞生物学];

学科分类号：

071009 ; 090102 ;

摘要：

Stathmin, a ubiquitous cytosolic phosphoprotein which may play a role in integrating the effects of diverse signals regulating proliferation, differentiation and other cell functions, was found to be phosphorylated rapidly and stoichiometrically by mitogen-activated protein (MAP) kinase in vitro. Ser-25 was identified as the major site and Ser-38 as a minor site of phosphorylation, while the p42 and p44 isoforms of MAP kinase were the only significant stathmin kinases detected in PC12 cells after stimulation by nerve growth factor (NGF). The results suggest that MAP kinases are the enzymes responsible for increasing the level of phosphorylation of Ser-25, which has been observed previously in PC12 cells following stimulation by NGF.

引用

页码：151 / 156

页数：6

共 32 条

[1] REQUIREMENT FOR INTEGRATION OF SIGNALS FROM 2 DISTINCT PHOSPHORYLATION PATHWAYS FOR ACTIVATION OF MAP KINASE [J].