Mitogen inactivation of glycogen synthase kinase-3 beta in intact cells via serine 9 phosphorylation.
Biochem J
; 303 ( Pt 3): 701-4, 1994 Nov 01.
Article
em En
| MEDLINE
| ID: mdl-7980435
ABSTRACT
Glycogen synthase kinase-3 (GSK-3), a protein-serine kinase implicated in cell-fate determination and differentiation, phosphorylates several regulatory proteins that are activated by dephosphorylation in response to hormones or growth factors. GSK-3 beta is phosphorylated in vitro at serine 9 by p70 S6 kinase and p90rsk-1, resulting in its inhibition [Sutherland, Leighton, and Cohen (1993) Biochem. J. 296, 15-19]. Using HeLa cells expressing GSK-3 beta or a mutant containing alanine at residue 9, we demonstrate that serine 9 is modified in intact cells and is targeted specifically by p90rsk-1, and that phosphorylation leads to loss of activity. Since p90rsk-1 is directly activated by mitogen-activated protein kinases, agonists of this pathway, such as insulin, repress GSK-3 function.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Serina
/
Proteínas Quinases Dependentes de Cálcio-Calmodulina
/
Mitógenos
Limite:
Humans
Idioma:
En
Ano de publicação:
1994
Tipo de documento:
Article