Regulation of GSK3 isoforms by phosphatases PP1 and PP2A

被引：68
|
作者：
Hernandez, Felix [1 ]
Langa, Elena [1 ]
Cuadros, Raquel [1 ]
Avila, Jesus [1 ,2 ]
Villanueva, Nieves [3 ]
机构：
[1] Ctr Biol Mol Severo Ochoa CSIC UAM, Madrid 28049, Spain
[2] CIBERNED, Madrid 28031, Spain
[3] Inst Salud Carlos III, Ctr Nacl Microbiol, Madrid 28220, Spain
来源：
MOLECULAR AND CELLULAR BIOCHEMISTRY | 2010年 / 344卷 / 1-2期
关键词：
GSK-3; PP1; PP2A; Okadaic acid; Lithium; GLYCOGEN-SYNTHASE KINASE-3-BETA; PHOSPHORYLATION; KINASE; INACTIVATION; PROTEIN; LITHIUM; CELLS; NEURONS; ROLES;
D O I：
10.1007/s11010-010-0544-0
中图分类号：
Q2 [细胞生物学];
学科分类号：
071009 ; 090102 ;
摘要：
Dephosphorylation of phospho GSK3 isoforms, from COS-7 cells, was determined in vitro and in cultured cells in the absence or the presence of okadaic acid and lithium. Our results indicate a preferential dephosphorylation of phospho GSK3 alpha by PP2A phosphatase, whereas dephosphorylation of phospho GSK3 beta mainly takes place by PP1 phosphatase.
引用
收藏
页码：211 / 215
页数：5
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