E1AF degradation by a ubiquitin-proteasome pathway

被引：15
|
作者：
Takahashi, A
Higashino, F
Aoyagi, M
Yoshida, K
Itoh, M
Kobayashi, M
Totsuka, Y
Kohgo, T
Shindoh, M
机构：
[1] Hokkaido Univ, Grad Sch Dent Med, Dept Oral Pathobiol Sci, Kita Ku, Sapporo, Hokkaido 0608586, Japan
[2] Sapporo Med Univ, Dept Biol, Sch Med, Chuo Ku, Sapporo, Hokkaido 0608556, Japan
[3] Hokkaido Univ, Div Canc Pathobiol, Inst Med Genet, Kita Ku, Sapporo, Hokkaido 0600815, Japan
来源：
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2005年 / 327卷 / 02期
关键词：
E1AF; ETS; PEA3; proteasome; ubiquitin; degradation;
D O I：
10.1016/j.bbrc.2004.12.045
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
E1AF is a member of the ETS family of transcription factors. In mammary tumors. overexpression of E1AF is associated with tumorigenesis, but E1AF protein has hardly been detected and its degradation mechanism is not yet clear. Here we show that E1AF protein is stabilized by treatment with the 26S protease inhibitor MG132. We found that E1AF was modified by ubiquitin through the C-terminal region and ubiquitinated E1AF aggregated in nuclear dots, and that the inhibition of proteasome-activated transcription from E1AF target promoters. These results suggest that E1AF is degraded via the ubiquitin-proteasome pathway. which has some effect on E1AF function. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码：575 / 580
页数：6
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