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ACTIVATION OF P34CDC2 KINASE BY CYCLIN IS NEGATIVELY REGULATED BY CYCLIC AMP-DEPENDENT PROTEIN-KINASE IN XENOPUS-OOCYTES
被引:43
作者:
RIME, H
HACCARD, O
OZON, R
机构:
[1] Laboratoire de Physiologie de la Reproduction, UA-CNRS, INRA 1449, Université P. et M. Curie. 4, Place Jussieu
关键词:
D O I:
10.1016/0012-1606(92)90217-5
中图分类号:
Q [生物科学];
学科分类号:
07 ;
0710 ;
09 ;
摘要:
Microinjection of a bacterially expressed stable Δ90 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), Δ90 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 Δ90 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. © 1992.
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页码:105 / 110
页数:6
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