E1AF degradation by a ubiquitin–proteasome pathway

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 pr...

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Bibliographic Details
Published in:Biochemical and biophysical research communications 2005-02, Vol.327 (2), p.575-580
Main Authors: Takahashi, Akiko, Higashino, Fumihiro, Aoyagi, Mariko, Yoshida, Koichi, Itoh, Miyuki, Kobayashi, Masanobu, Totsuka, Yasunori, Kohgo, Takao, Shindoh, Masanobu
Format: Article
Language:English
Subjects:
Adenovirus E1A Proteins - chemistry
Adenovirus E1A Proteins - genetics
Adenovirus E1A Proteins - metabolism
Animals
Cell Line
Cell Nucleus Structures - drug effects
Cell Nucleus Structures - metabolism
Cercopithecus aethiops
Degradation
E1AF
ETS
Humans
Leupeptins - pharmacology
Mice
PEA3
Promoter Regions, Genetic - genetics
Proteasome
Proteasome Endopeptidase Complex - metabolism
Proteasome Inhibitors
Proto-Oncogene Proteins - chemistry
Proto-Oncogene Proteins - genetics
Proto-Oncogene Proteins - metabolism
Transcription, Genetic - drug effects
Transcription, Genetic - genetics
Ubiquitin
Ubiquitin - metabolism
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Summary: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.
ISSN:0006-291X
1090-2104
DOI:10.1016/j.bbrc.2004.12.045