The transcription factor Krox20 is an E3 ligase that sumoylates its Nab coregulators
Covalent attachment of small ubiquitin-like modifier (SUMO) to proteins regulates many processes in the eukaryotic cell. This reaction is similar to ubiquitination and usually requires an E3 ligase for substrate modification. However, only a few SUMO ligases have been described so far, which frequen...
| Autores: | , , , , |
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| Tipo de recurso: | artículo |
| Estado: | Versión enviada para evaluación y publicación |
| Fecha de publicación: | 2011 |
| País: | España |
| Institución: | Consejo Superior de Investigaciones Científicas (CSIC) |
| Repositorio: | DIGITAL.CSIC. Repositorio Institucional del CSIC |
| OAI Identifier: | oai:digital.csic.es:10261/52347 |
| Acceso en línea: | http://hdl.handle.net/10261/52347 |
| Access Level: | acceso abierto |
| Palabra clave: | Krox20 Nab SUMO ligase Ubc9 |
| Sumario: | Covalent attachment of small ubiquitin-like modifier (SUMO) to proteins regulates many processes in the eukaryotic cell. This reaction is similar to ubiquitination and usually requires an E3 ligase for substrate modification. However, only a few SUMO ligases have been described so far, which frequently facilitate sumoylation by bringing together the SUMO-conjugating enzyme Ubc9 and the target protein. Ubc9 is an interaction partner of the transcription factor Krox20, a key regulator of hindbrain development. Here, we show that Krox20 functions as a SUMO ligase for its coregulators-the Nab proteins-and that Nab sumoylation negatively modulates Krox20 transcriptional activity in vivo. © 2011 EuropeEan MoleEcular Biology Oorganization. |
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