Ubiquitin-dependent degradation of adenovirus E1A protein is inhibited by BS69 - PubMed (original) (raw)
. 2006 Jan 6;339(1):367-74.
doi: 10.1016/j.bbrc.2005.11.028. Epub 2005 Nov 14.
Affiliations
- PMID: 16300738
- DOI: 10.1016/j.bbrc.2005.11.028
Ubiquitin-dependent degradation of adenovirus E1A protein is inhibited by BS69
Tomoyasu Isobe et al. Biochem Biophys Res Commun. 2006.
Abstract
Adenovirus E1A protein perturbs the cell cycle and promotes cell transformation. Although E1A is relatively unstable, regulation of E1A stability has not been fully elucidated. Here, we showed that E1A was ubiquitinated and degraded using a proteasome in vivo system. Interestingly, we found that BS69, one of the E1A-binding proteins, inhibited ubiquitination of E1A. BS69 mutants lacking the MYND domain could not bind to E1A and did not inhibit ubiquitination of E1A. Moreover, we demonstrated that overexpression of BS69 stabilized E1A in vivo. These results suggest that BS69 controls E1A stability via inhibition of ubiquitination.