| Cyclin A-Cdk2 Phosphorylates BH3 only Protein Bad in vitro and in vivo |
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| 引用本文： | HE Kan CHEN Yue LI Jing-hua ZHAN Zhuo WU Yong-ge KONG Wei JIN Ying-hua. Cyclin A-Cdk2 Phosphorylates BH3 only Protein Bad in vitro and in vivo[J]. 高等学校化学研究, 2007, 23(5): 567-570. DOI: 10.1016/S1005-9040(07)60124-X |
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| 作者姓名： | HE Kan CHEN Yue LI Jing-hua ZHAN Zhuo WU Yong-ge KONG Wei JIN Ying-hua |
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| 作者单位： | [1]Vaccine Research Center, College of Life Science [2]Key Laboratory for Supramolecular Structure ＆ Materials of Ministry of Education, College of Life Science [3]School of Public Health, Jilin University, Changchun 130012, P. R. China |
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| 基金项目： | Supported by the National Natural Science Foundation of China （Nos. 30370294 and 30640064）. |
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| 摘 要： |
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| 关 键 词： | 细胞凋亡 细胞周期蛋白 A-Cdk2 磷酸化 基质 |
| 收稿时间： | 2007-02-09 |
| 修稿时间： | 2007-02-09 |
Cyclin A-Cdk2 Phosphorylates BH3 only Protein Bad in vitro and in vivo |
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| Kan HE, Yue CHEN, Jing-hua LI, Zhuo ZHAN, Yong-ge WU, Wei KONG,Ying-hua JIN,. Cyclin A-Cdk2 Phosphorylates BH3 only Protein Bad in vitro and in vivo[J]. Chemical Research in Chinese University, 2007, 23(5): 567-570. DOI: 10.1016/S1005-9040(07)60124-X |
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| Authors: | Kan HE Yue CHEN Jing-hua LI Zhuo ZHAN Yong-ge WU Wei KONG Ying-hua JIN |
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| Affiliation: | aVaccine Research Center, College of Life Science;bKey Laboratory for Supramolecular Structure & Materials of Ministry of Education;cSchool of Public Health, Jilin University, Changchun 130012, P. R. China |
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| Abstract: | Increasing evidence suggests that Cyclin A-Cdk2 activity is required in the apoptosis process induced by various stimuli. To determine a specific substrate of Cyclin A-Cdk2 for apoptosis, in this study, we carried out anin vitro kinase assay using immunoprecipitated complex Cyclin A-Cdk2 as an enzyme source, and recombinant protein GST-Bad as a substrate. Our study showed that Bad was clearly phosphorylated by Cyclin A-Cdk2 in vitro. To examine whether protein Bad can also be phosphorylated by Cyclin A-Cdk2 kinase in vivo, we transiently overexpressed protein Bad with Cyclin A or Cdk2-dn, a dominant negative version of Cdk2, in Hela cells and determined the phosphorylation status of protein Bad. The test showed that protein Bad was clearly phosphorylated in Cyclin A overexpressed cells,but not in Cdk2-dn or mock transfectent. Moreover, etoposide also caused the phosphorylation of endogenetic Bad. In conclusion, here we provide first time evidence that protein Bad can be a substrate of Cyclin A-Cdk2 apoptosis for in vitro and in vivo. |
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| Keywords: | Apoptosis Bad Cyclin A-Cdk2 Phosphorylation Substrate |
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