Abstract:
:ATF5 is a member of the CREB/ATF family of transcription factors. In the current study, using a transient transfection system to express FLAG epitope fusion proteins of ATF5, we have shown that CdCl(2) or NaAsO(3) increases the protein levels of ATF5 in cells, and that cadmium stabilizes the ATF5 protein. Proteasome inhibitors had a similar effect to cadmium on the cellular accumulation of ATF5. Proteasome inhibition led to an increase in ubiquitinated ATF5, while cadmium did not appear to reduce the extent of ATF5 ubiquitination. ATF5 contains a putative nuclear export signal within its N-terminus. We demonstrated that whereas deletion of N-terminal region resulted in a increase of ATF5 levels, this region does not appear to be involved in the ubiquitination of ATF5. These results indicate that ATF5 is targeted for degradation by the ubiquitin-proteasome pathway, and that cadmium slows the rate of ATF5 degradation via a post-ubiquitination mechanism.
journal_name
Biochem Biophys Res Communjournal_title
Biochemical and biophysical research communicationsauthors
Uekusa H,Namimatsu M,Hiwatashi Y,Akimoto T,Nishida T,Takahashi S,Takahashi Ydoi
10.1016/j.bbrc.2009.01.158subject
Has Abstractpub_date
2009-03-13 00:00:00pages
673-8issue
3eissn
0006-291Xissn
1090-2104pii
S0006-291X(09)00206-Xjournal_volume
380pub_type
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