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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Mortensen, Franziska Barbic, Tanja Schneider, Daniel Marx, Andreas Sladewska-marquardt, Anna Kühnle, Simone Scheffner, Martin |
| Description | Author Affiliation: Mortensen F ( Department of Biology, University of Konstanz, 78457 Konstanz, Germany); Schneider D ( Department of Biology, University of Konstanz, 78457 Konstanz, Germany); Barbic T ( Department of Biology, University of Konstanz, 78457 Konstanz, Germany); Sladewska-Marquardt A ( Department of Biology, University of Konstanz, 78457 Konstanz, Germany); Kühnle S ( Department of Biology, University of Konstanz, 78457 Konstanz, Germany); Marx A ( Konstanz Research School Chemical Biology, University of Konstanz, 78457 Konstanz, Germany); Scheffner M ( Department of Biology, University of Konstanz, 78457 Konstanz, Germany); |
| Abstract | Deregulation of the ubiquitin ligase E6 associated protein (E6AP) encoded by the UBE3A gene has been associated with three different clinical pictures. Hijacking of E6AP by the E6 oncoprotein of distinct human papillomaviruses (HPV) contributes to the development of cervical cancer, whereas loss of E6AP expression or function is the cause of Angelman syndrome, a neurodevelopmental disorder, and increased expression of E6AP has been involved in autism spectrum disorders. Although these observations indicate that the activity of E6AP has to be tightly controlled, only little is known about how E6AP is regulated at the posttranslational level. Here, we provide evidence that the hydrophobic patch of ubiquitin comprising Leu-8 and Ile-44 is important for E6AP-mediated ubiquitination, whereas it does not affect the catalytic properties of the isolated catalytic HECT domain of E6AP. Furthermore, we show that the HPV E6 oncoprotein rescues the disability of full-length E6AP to use a respective hydrophobic patch mutant of ubiquitin for ubiquitination and that it stimulates E6AP-mediated ubiquitination of Ring1B, a known substrate of E6AP, in vitro and in cells. Based on these data, we propose that E6AP exists in at least two different states, an active and a less active or latent one, and that the activity of E6AP is controlled by noncovalent interactions with ubiquitin and allosteric activators such as the HPV E6 oncoprotein. |
| ISSN | 00278424 |
| e-ISSN | 10916490 |
| Journal | Proceedings of the National Academy of Sciences of the United States of America |
| Issue Number | 32 |
| Volume Number | 112 |
| Language | English |
| Publisher | National Academy of Sciences |
| Publisher Date | 2015-08-01 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Ubiquitin-Protein Ligases Metabolism Ubiquitin Ubiquitination Allosteric Regulation Amino Acid Sequence Biocatalysis Cell Line, Tumor Cysteine Hydrophobic And Hydrophilic Interactions Molecular Sequence Data Peptides Protein Binding Protein Structure, Tertiary Chemistry Ubiquitin-Conjugating Enzymes Research Support, Non-U.S. Gov't Multidisciplinary |
| Content Type | Text |
| Resource Type | Article |
| Subject | Multidisciplinary |
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