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Purification of Ubiquitinated p53 Proteins from Mammalian Cells
10:55

Purification of Ubiquitinated p53 Proteins from Mammalian Cells

Published on: March 21, 2022

Identification and characterization of murine mHAUSP encoding a deubiquitinating enzyme that regulates the status of

Soo-Kyung Lim1, Ju-Mi Shin, Yong-Soo Kim

  • 1Cell and Gene Therapy Research Institute, Pochon CHA University, CHA General Hospital, Seoul, Korea.

International Journal of Oncology
|January 14, 2004
PubMed

Insights

Researchers identified mHAUSP, a mouse protein that deubiquitinates and stabilizes the p53 protein. This discovery sheds light on the regulation of p53 stability and function in mice.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Herpesvirus-associated ubiquitin-specific protease (HAUSP) interacts with and deubiquitinates human p53.
  • Human HAUSP stabilizes p53, promoting cell growth repression and apoptosis.

Purpose of the Study:

  • To isolate and characterize the mouse orthologue of HAUSP (mHAUSP).
  • To investigate the deubiquitinating activity of mHAUSP, particularly on p53.

Main Methods:

  • Cloning of mHAUSP cDNA from mouse ES cells using RT-PCR.
  • Northern blot analysis to determine transcript expression patterns.
  • In vivo and in vitro deubiquitinating enzyme assays.

Main Results:

  • mHAUSP cDNA encodes a 1,103-amino acid protein with conserved deubiquitinating enzyme domains.
  • mHAUSP exhibits deubiquitinating enzyme activity.
  • Overexpression of mHAUSP reduces ubiquitinated p53 levels, confirming its role in p53 deubiquitination.

Conclusions:

  • mHAUSP is a functional mouse orthologue of human HAUSP.
  • mHAUSP deubiquitinates p53, suggesting a conserved mechanism for p53 regulation in mammals.

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