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HAUSP, a deubiquitinating enzyme for p53, is polyubiquitinated, polyneddylated, and dimerized

Authors :
Lee, Hye-Jin
Kim, Myung-Sun
Kim, Yu-Kyung
Oh, Yu-Kyoung
Baek, Kwang-Hyun
Source :
FEBS Letters; Aug2005, Vol. 579 Issue 21, p4867-4872, 6p
Publication Year :
2005

Abstract

Abstract: The tumor suppressor protein p53 is ubiquitinated and neddylated by MDM2 and then degraded by 26S proteasome. However, p53 is stabilized by the HAUSP (Herpes-virus-associated ubiquitin-specific protease) deubiquitinating enzyme. In this study, we discovered that rat HAUSP (rHAUSP) is polyubiquitinated, polyneddylated, and dimerized using co-immunoprecipitation assays. This suggests that rHAUSP may function as a dimer or multimer and is also degraded through the proteasome-mediated degradation. Transfection of rHAUSP into RGC-Lac-Z cell line with the integrated p53 response element revealed that rHAUSP contributed to p53 stabilization, and a rHAUSP (C224S) mutant contributed to p53 destabilization in a dose-dependent manner. [Copyright &y& Elsevier]

Details

Language :
English
ISSN :
00145793
Volume :
579
Issue :
21
Database :
Complementary Index
Journal :
FEBS Letters
Publication Type :
Academic Journal
Accession number :
18244110
Full Text :
https://doi.org/10.1016/j.febslet.2005.07.048