Abstract
Cell proliferation is controlled by cdk2 which in association with cyclin E and A regulates G1/S transition and S phase progression. cdk2 activation is dependent on its localization in the nucleus where regulatory mediators are found. We report that activation of cdk2 is associated with the formation of cdk2/MAP Kinase complexes. cdk2 associates with both inactive and activated MAP Kinase. Prevention of MAP Kinase activation by the MEK inhibitor PD98059 inhibits both activation and nuclear localization of cdk2 and S phase entry. These findings indicate that the nuclear translocation of cdk2 is associated with the formation of molecular complexes containing active MAP Kinase and is dependent on MAP Kinase activation.
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Acknowledgements
We would like to thank Dr T Hori and Dr J Pierre for the gift of Kit 225 cells and recombinant Elk1 respectively. We also thank N Avazeri for very useful technical assistance. This work was supported by INSERM and grants from the Association pour la Recherche sur le Cancer (ARC, Villejuif, France). DA Blanchard receives a fellowship from ARC.
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Blanchard, D., Mouhamad, S., Auffredou, MT. et al. Cdk2 associates with MAP Kinase in vivo and its nuclear translocation is dependent on MAP Kinase activation in IL-2-dependent Kit 225 T lymphocytes. Oncogene 19, 4184–4189 (2000). https://doi.org/10.1038/sj.onc.1203761
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DOI: https://doi.org/10.1038/sj.onc.1203761
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