Ha-rasVal-12,Thr-59 activates S6 kinase and p34cdc2 kinase in Xenopus oocytes: evidence for c-mosxe-dependent and -independent pathways
Autor: | C B Barrett, F A van der Hoorn, James L. Maller, R M Schroetke, Steven K. Nordeen |
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Rok vydání: | 1990 |
Předmět: |
Ribosomal Proteins
Maturation-Promoting Factor Oligonucleotides Protamine Kinase Oncogene Protein p21(ras) Mitogen-activated protein kinase kinase MAP2K7 Xenopus laevis Proto-Oncogene Proteins Animals Insulin Growth Substances Molecular Biology Progesterone Ribosomal Protein S6 Germinal vesicle biology Ribosomal Protein S6 Kinases Cyclin-dependent kinase 5 Cyclin-dependent kinase 2 Cyclin-dependent kinase 3 Cell Biology Oligonucleotides Antisense Molecular biology Protein kinase R Enzyme Activation Proto-Oncogene Proteins c-mos Oocytes biology.protein Cyclin-dependent kinase 9 Protein Kinases Research Article |
Zdroj: | Molecular and Cellular Biology. 10:310-315 |
ISSN: | 1098-5549 0270-7306 |
DOI: | 10.1128/mcb.10.1.310 |
Popis: | Treatment with insulin or progesterone or microinjection of the transforming protein product of Ha-rasVal-12,Thr-59 (p21) is known to induce germinal vesicle breakdown in Xenopus oocytes. We have investigated the effect of p21 on S6 kinase and the H1 histone kinase of maturation-promoting factor in the presence and absence of antisense oligonucleotides against the c-mosxe proto-oncogene. Injection of p21 led to a rapid increase in S6 phosphorylation, with kinetics similar to those previously observed with insulin. Microinjection of c-mosxe antisense oligonucleotides inhibited germinal vesicle breakdown induced by p21 and totally abolished S6 kinase activation by insulin or progesterone but only partially inhibited activation by p21. However, the activation of p34cdc2 protein kinase by all three stimuli was blocked by antisense oligonucleotides. The results suggest that in oocyte maturation c-mosxe functions downstream of p21 but upstream of p34cdc2 and S6 kinase activation, although not all p21-induced events require c-mosxe. |
Databáze: | OpenAIRE |
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