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Purification of Ubiquitinated p53 Proteins from Mammalian Cells
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VprBP/DCAF1 regulates p53 function and stability through site-specific phosphorylation.

Nikhil Baban Ghate1, Sungmin Kim1, Roasa Mehmood1

  • 1Department of Biochemistry and Molecular Medicine, Norris Comprehensive Cancer Center, University of Southern California, Los Angeles, CA, 90033, USA.

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|April 11, 2023
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Summary
This summary is machine-generated.

VprBP (Vpr-binding protein) phosphorylates p53 at serine 367, inhibiting its tumor-suppressing activity and promoting cancer growth. This phosphorylation event also targets p53 for degradation, highlighting VprBP as a key regulator in tumorigenesis.

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Area of Science:

  • Molecular Biology
  • Cancer Biology
  • Biochemistry

Background:

  • VprBP (DCAF1) is an overexpressed kinase in cancer, linked to gene silencing and tumorigenesis.
  • VprBP's role in histone H2A phosphorylation is established, but its non-histone targets and oncogenic signaling roles are unexplored.

Purpose of the Study:

  • To investigate if VprBP phosphorylates non-histone proteins.
  • To determine the role of VprBP-mediated phosphorylation in oncogenic signaling pathways.
  • To elucidate the mechanism by which VprBP influences p53 function and stability.

Main Methods:

  • Investigated VprBP's interaction with p53.
  • Analyzed the effect of VprBP on p53 phosphorylation at serine 367 (S367p).
  • Assessed the impact of p53S367p on p53 transcriptional activity, growth suppression, and proteasomal degradation.
  • Examined the role of p53 acetylation in regulating VprBP-p53 interaction and p53 function.

Main Results:

  • VprBP directly interacts with p53's C-terminal domain to catalyze p53S367p.
  • VprBP-mediated p53S367p attenuates p53's transcriptional and growth-suppressive activities.
  • p53S367p promotes p53 proteasomal degradation, reducing p53 protein levels and transactivation.
  • p53 acetylation abrogates VprBP-p53 interaction, preventing p53S367p and enhancing p53 function in response to DNA damage.

Conclusions:

  • VprBP acts as a negative regulator of p53 function through S367 phosphorylation.
  • VprBP-mediated p53S367p is a novel mechanism that modulates p53 stability and promotes tumorigenesis.
  • Targeting the VprBP-p53 interaction offers a potential therapeutic strategy for cancer treatment.