Regulation of GSK3 isoforms by phosphatases PP1 and PP2A.
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 GSK3α by PP2A phosphatase, whereas dephosphorylation of phospho GSK3β mainly takes place by PP1 phosphatase.
Hernández
Félix
F
Centro de Biologia Molecular Severo Ochoa (CSIC-UAM), Madrid, Spain.
Langa
Elena
E
Cuadros
Raquel
R
Avila
Jesús
J
Villanueva
Nieves
N
D000818:Animals; D019556:COS Cells; D002522:Chlorocebus aethiops; D038362:Glycogen Synthase Kinase 3 / Q000378:metabolism*; D007527:Isoenzymes / Q000378:metabolism*; D010749:Phosphoprotein Phosphatases / Q000378:metabolism*; D010766:Phosphorylation
D007527:Isoenzymes; D038362:Glycogen Synthase Kinase 3; D010749:Phosphoprotein Phosphatases