Activation of p34cdc2 kinase by cyclin is negatively regulated by cyclic amp-dependent protein kinase in Xenopus oocytes.
Dev Biol
; 151(1): 105-10, 1992 May.
Article
en En
| MEDLINE
| ID: mdl-1533599
Microinjection of a bacterially expressed stable delta 90 sea urchin cyclin B into Xenopus prophase oocytes, in absence or presence of cycloheximide, provokes the activation of histone H1 kinase and the tyrosine dephosphorylation of p34cdc2. Unexpectedly, when prophase oocytes are submitted to a treatment known to elevate the intracellular cAMP level (3-isobutyl-1-methylxanthine and cholera toxin), delta 90 cyclin has no effect and the oocytes remain blocked in prophase. This inhibition is reverted by the microinjection of the inhibitor of cAMP-dependent protein kinase. When delta 90 cyclin is microinjected into oocytes depleted of endogenous cyclins (cycloheximide-treated metaphase I) and in the presence of a high intracellular concentration of cAMP, p34cdc2 kinase is tyrosine rephosphorylated. Altogether, our results indicate that in Xenopus oocyte, cAMP-dependent protein kinase (A-kinase) controls the formation of the cyclin B/p34cdc2 complex which remains inactive and tyrosine phosphorylated.
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Colección:
01-internacional
Base de datos:
MEDLINE
Asunto principal:
Oocitos
/
Proteínas Quinasas
/
Proteína Quinasa CDC2
/
Ciclinas
Límite:
Animals
Idioma:
En
Revista:
Dev Biol
Año:
1992
Tipo del documento:
Article
País de afiliación:
Francia
Pais de publicación:
Estados Unidos