Cdk9 phosphorylates p53 on serine 392 independently of CKII.

  title={Cdk9 phosphorylates p53 on serine 392 independently of CKII.},
  author={Pier Paolo Claudio and Jianqi Cui and Mohammad Ghafouri and Chiara Mariano and Martyn K. White and Mahmut Safak and Joel B. Sheffield and Antonio Giordano and Kamel Khalili and Shohreh Amini and Bassel E. Sawaya},
  journal={Journal of cellular physiology},
  volume={208 3},
The tumor suppressor p53 is an important cellular protein, which controls cell cycle progression. Phosphorylation is one of the mechanisms by which p53 is regulated. Here we report the interaction of p53 with another key regulator, cdk9, which together with cyclin T1 forms the positive transcription elongation complex, p-TEFb. This complex cooperates with the HIV-1 Tat protein to cause the phosphorylation of the carboxyl terminal domain (CTD) of RNA polymerase II and this facilitates the… CONTINUE READING
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