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Title: USP3 stabilizes p53 protein through its deubiquitinase activity

Abstract

p53 is the guardian of the genome integrity and the degradation of p53 protein is mediated by MDM2. Here we report that USP3 interacts with p53 and regulates p53 stability. Depletion of USP3 lead to accelerated degradation of p53 in normal cells thereby enhanced cell proliferation and transformation. Reconstitution of wildtype USP3, but not the USP3 C168S mutant, restored the stability of p53 protein and inhibited cell proliferation and transformation. These findings suggest that USP3 is an important regulator of p53 and regulates normal cell transformation. - Highlights: • USP3 is a deubiquitinase for p53 and antagonizes Mdm2. • USP3 stabilizes p53 protein under normal condition. • Loss of USP3 accelerates cell proliferation and transformation.

Authors:
; ; ; ; ; ; ;  [1];  [2]
  1. Department of Spine and Spinal Cord Surgery, Wendeng Orthopaedic Hospital, Weihai, Shandong, 264400 (China)
  2. Department of Neurology, The Affiliated Weihai Central Hospital of Weifang Medical College, Weihai, Shandong, 264400 (China)
Publication Date:
OSTI Identifier:
22719104
Resource Type:
Journal Article
Journal Name:
Biochemical and Biophysical Research Communications
Additional Journal Information:
Journal Volume: 492; Journal Issue: 2; Other Information: Copyright (c) 2017 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved.; Country of input: International Atomic Energy Agency (IAEA); Journal ID: ISSN 0006-291X
Country of Publication:
United States
Language:
English
Subject:
60 APPLIED LIFE SCIENCES; CELL PROLIFERATION; CELL TRANSFORMATIONS; MUTANTS; PROTEINS; STABILITY

Citation Formats

Fu, Song, Shao, Shize, Wang, Longqiang, Liu, Haijun, Hou, Haitao, Wang, Yanan, Wang, Huan, Huang, Xiangpeng, and Lv, Renhua. USP3 stabilizes p53 protein through its deubiquitinase activity. United States: N. p., 2017. Web. doi:10.1016/J.BBRC.2017.08.036.
Fu, Song, Shao, Shize, Wang, Longqiang, Liu, Haijun, Hou, Haitao, Wang, Yanan, Wang, Huan, Huang, Xiangpeng, & Lv, Renhua. USP3 stabilizes p53 protein through its deubiquitinase activity. United States. https://doi.org/10.1016/J.BBRC.2017.08.036
Fu, Song, Shao, Shize, Wang, Longqiang, Liu, Haijun, Hou, Haitao, Wang, Yanan, Wang, Huan, Huang, Xiangpeng, and Lv, Renhua. 2017. "USP3 stabilizes p53 protein through its deubiquitinase activity". United States. https://doi.org/10.1016/J.BBRC.2017.08.036.
@article{osti_22719104,
title = {USP3 stabilizes p53 protein through its deubiquitinase activity},
author = {Fu, Song and Shao, Shize and Wang, Longqiang and Liu, Haijun and Hou, Haitao and Wang, Yanan and Wang, Huan and Huang, Xiangpeng and Lv, Renhua},
abstractNote = {p53 is the guardian of the genome integrity and the degradation of p53 protein is mediated by MDM2. Here we report that USP3 interacts with p53 and regulates p53 stability. Depletion of USP3 lead to accelerated degradation of p53 in normal cells thereby enhanced cell proliferation and transformation. Reconstitution of wildtype USP3, but not the USP3 C168S mutant, restored the stability of p53 protein and inhibited cell proliferation and transformation. These findings suggest that USP3 is an important regulator of p53 and regulates normal cell transformation. - Highlights: • USP3 is a deubiquitinase for p53 and antagonizes Mdm2. • USP3 stabilizes p53 protein under normal condition. • Loss of USP3 accelerates cell proliferation and transformation.},
doi = {10.1016/J.BBRC.2017.08.036},
url = {https://www.osti.gov/biblio/22719104}, journal = {Biochemical and Biophysical Research Communications},
issn = {0006-291X},
number = 2,
volume = 492,
place = {United States},
year = {Sat Oct 14 00:00:00 EDT 2017},
month = {Sat Oct 14 00:00:00 EDT 2017}
}