Blanchette, Paola and Cheng, Chi Ying and Yan, Qin and Ketner, Gary and Ornelles, David A. and Dobner, Thomas and Conaway, Ronald C. and Conaway, Joan Weliky and Branton, Philip E. (2004) Both BC-Box motifs of adenovirus protein E4orf6 are required to efficiently assemble an E3 ligase complex that degrades p53. MOLECULAR AND CELLULAR BIOLOGY, 24 (21). pp. 9619-9629. ISSN 0270-7306, 1098-5549
Full text not available from this repository. (Request a copy)Abstract
Small DNA tumor viruses typically encode proteins that either inactivate or degrade p53. Human adenoviruses encode products, including E4orf6 and E1B55K, that do both. Each independently binds to p53 and inhibits its ability to activate gene expression; however, in combination they induce p53 degradation by the ubiquitin pathway. We have shown previously that p53 degradation relies on interactions of E4orf6 with the cellular proteins Cul5, Rbx1, and elongins B and C to form an E3 ligase similar to the SCF and VBC complexes. Here we show that, like other elongin BC-interacting proteins, including elongin A, von Hippel-Lindau protein, and Muf1, the interaction of E4orf6 is mediated by the BC-box motif; however, E4orf6 uniquely utilizes two BC-box motifs for degradation of p53 and another target, Mre11. In addition, our data suggest that the interaction of E1B55K with E4orf6 depends on the ability of E4orf6 to form the E3 ligase complex and that such complex formation may be required for all E4orf6-E1B55K functions.
| Item Type: | Article |
|---|---|
| Uncontrolled Keywords: | TUMOR-SUPPRESSOR PROTEIN; PAPILLOMAVIRUS E6 PROTEINS; E1B 55-KILODALTON PROTEIN; SCF UBIQUITIN LIGASE; LATE GENE-EXPRESSION; INFECTED-CELLS; ELONGIN-C; MEDIATED DEGRADATION; NUCLEAR-LOCALIZATION; MESSENGER-RNA; |
| Subjects: | 600 Technology > 610 Medical sciences Medicine |
| Divisions: | Medicine > Lehrstuhl für Medizinische Mikrobiologie und Hygiene |
| Depositing User: | Dr. Gernot Deinzer |
| Date Deposited: | 23 Jun 2021 08:14 |
| Last Modified: | 23 Jun 2021 08:14 |
| URI: | https://pred.uni-regensburg.de/id/eprint/37012 |
Actions (login required)
 |
View Item |
