Degradation of Cyclin A Does Not Require Its Phosphorylation by CDC2 and Cyclin-dependent Kinase 2*

@article{Yam2000DegradationOC,
  title={Degradation of Cyclin A Does Not Require Its Phosphorylation by CDC2 and Cyclin-dependent Kinase 2*},
  author={C. Yam and W. Y. Siu and A. Lau and R. Poon},
  journal={The Journal of Biological Chemistry},
  year={2000},
  volume={275},
  pages={3158 - 3167}
}
Many cyclins are degraded by the ubiquitination/proteasome pathways involving the anaphase-promoting complex and SCF complexes. These degradations are frequently dependent on phosphorylation by cyclin-dependent kinases (CDKs), providing a self-limiting mechanism for CDK activity. Here we present evidence from in vitro and in vivo assay systems that the degradation of human cyclin A can be inhibited by kinase-inactive mutants of CDK2 and CDC2. One obvious interpretation of these results is that… Expand
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