Jaumot M, Estañol J M, Casanovas O, Graña X, Agell N, Bachs O
Department of Cell Biology, Faculty of Medicine, University of Barcelona, Spain.
Biochem Biophys Res Commun. 1997 Dec 18;241(2):434-8. doi: 10.1006/bbrc.1997.7787.
We report here experimental evidence indicating that the p21CIP, the universal inhibitor of cyclin-dependent protein kinases, general inhibitor CDKs is a substrate oof cyclin A-cdk2. The evidence comes from phosphorylation experiments in which the endogenous p21CIP present in using the original cyclin A-cdk2 complexes immunoprecipitated from HeLa cells extracts can be phosphorylated by the cdk2 of the same complexes. In vitro experiments showing that reconstituted GSTcyclin A-GSTcdk2 complexes from phosphorylate recombinant GSTp21CIP confirms that p21CIP is a cyclin A-cdk2 substrate.
我们在此报告实验证据,表明细胞周期蛋白依赖性蛋白激酶的通用抑制剂p21CIP是细胞周期蛋白A-cdk2的底物。该证据来自磷酸化实验,其中从HeLa细胞提取物中免疫沉淀的原始细胞周期蛋白A-cdk2复合物中存在的内源性p21CIP可被相同复合物的cdk2磷酸化。体外实验表明,重组的GST细胞周期蛋白A-GSTcdk2复合物可磷酸化重组GSTp21CIP,这证实了p21CIP是细胞周期蛋白A-cdk2的底物。