Impact of Mdm2-p53 on the proteasome assembly and disassembly Role of the ubiquitination of some 19S subunits
Abstract:
The ubiquitin proteasome system is a fundamental actor for the proteolysis of cellular proteins. My results demonstrated that the E3 ligase Mdm2 and its substrate p53 might be implied in the formation of the fully-assembled proteasome. Mdm2 promotes also the ubiquitination of some 19S subunits of the proteasome via a non-conventional chain and it is not a signal for self-degradation. Moreover, this ubiqitination seemed to play a role in the formation of the proteasome.
| Zugehörige Institution(en) am KIT | Institut für Toxikologie und Genetik (ITG) |
| Publikationstyp | Hochschulschrift |
| Publikationsjahr | 2011 |
| Sprache | Englisch |
| Identifikator | urn:nbn:de:swb:90-248120 KITopen-ID: 1000024812 |
| Verlag | Karlsruher Institut für Technologie (KIT) |
| Art der Arbeit | Dissertation |
| Fakultät | Fakultät für Chemie und Biowissenschaften (CHEM-BIO) |
| Institut | Institut für Toxikologie und Genetik (ITG) |
| Prüfungsdaten | 18.10.2011 |
| Schlagwörter | E3 liagase, Mdm2, p53, ubiquitin, 19S and 26S proteasomes |
| Nachgewiesen in | OpenAlex |
| Referent/Betreuer | Blattner, C. |