title: Regulation of GSK3 isoforms by phosphatases PP1 and PP2A.
abstract: 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.
authors.affiliation: Centro de Biologia Molecular Severo Ochoa (CSIC-UAM), Madrid, Spain.
authors.forename: Félix
authors.initials: F
authors.lastname: Hernández
authors.forename: Elena
authors.initials: E
authors.lastname: Langa
authors.forename: Raquel
authors.initials: R
authors.lastname: Cuadros
authors.forename: Jesús
authors.initials: J
authors.lastname: Avila
authors.forename: Nieves
authors.initials: N
authors.lastname: Villanueva
mesh_terms: 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
chemical_list: D007527:Isoenzymes; D038362:Glycogen Synthase Kinase 3; D010749:Phosphoprotein Phosphatases