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Phosphorylation status and function of P53 are inversely related to protein kinase C activation

K Nakamura1, Y Sun, Y Yokoyama

  • 1Gene Regulation Section, National Cancer Institute, Frederick Cancer Research and Development Center, MD 21702, USA. lfp51193@mwu.mukogawa-u.ac.jp

Anticancer Research
|April 19, 2000
PubMed

Insights

Protein kinase C (PKC) activity inversely affects p53 protein phosphorylation. Inhibiting PKC with H7 increased p53 phosphorylation, while activating it with TPA decreased it, impacting p53

Area of Science:

  • Molecular Biology
  • Cellular Signaling
  • Cancer Research

Background:

  • The regulation of p53 protein function through phosphorylation is not well understood.
  • Protein kinase C (PKC) is a key enzyme in cellular signaling pathways.

Purpose of the Study:

  • To investigate the role of PKC in the phosphorylation of p53 protein.
  • To determine how PKC activation or inhibition affects p53 protein phosphorylation and its transcriptional activity.

Main Methods:

  • Mouse epidermal JB6 cells were treated with PKC inhibitor (H7) or activator (TPA).
  • p53 protein phosphorylation levels were assessed in vivo.
  • Transient transfection/luciferase reporter assays were used to measure MDM2 reporter transactivation activity.

Main Results:

  • H7 treatment increased wild-type p53 phosphorylation, while TPA decreased it.
  • Forskolin (PKA activator) did not affect p53 phosphorylation.
  • H7 modestly increased p53 transactivation activity, whereas TPA completely blocked it.

Conclusions:

  • p53 phosphorylation is inversely related to PKC activation.
  • p53 phosphorylation may play a role in its function as a transcription factor.

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