HDAC6 mediates the acetylation of TRIM50
| Autor: | Giuseppe Merla, Flora Cozzolino, Carmela Fusco, Piero Pucci, Pasquelena De Nittis, Barbara Mandriani, Maria Chiara Monti, Bartolomeo Augello, Maria Teresa Pellico, Alessia Calcagnì, Lucia Micale |
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| Přispěvatelé: | Fusco, C, Micale, L, Augello, B, Mandriani, B, Pellico, Mt, De Nittis, P, Calcagnì, A, Monti, Maria, Cozzolino, Flora, Pucci, Pietro, Merla, G. |
| Rok vydání: | 2013 |
| Předmět: |
Ubiquitin-Protein Ligases
Histone Deacetylase 6 Microtubules Histone Deacetylases Cell Line Tripartite Motif Proteins Mice Ubiquitin Animals Humans p300-CBP Transcription Factors biology Chemistry Ubiquitination Acetyltransferases Acetylation Cell Biology HDAC6 Molecular biology Ubiquitin ligase Cell biology Protein Structure Tertiary Aggresome Tubulin HEK293 Cells PCAF biology.protein HeLa Cells Protein Binding |
| Zdroj: | Cellular signalling. 26(2) |
| ISSN: | 1873-3913 |
| Popis: | The E3 Ubiquitin ligase TRIM50 promotes the formation and clearance of aggresome-associated polyubiquitinated proteins through HDAC6 interaction, a tubulin specific deacetylase that regulates microtubule-dependent aggresome formation. In this report we showed that TRIM50 is a target of HDAC6 with Lys-372 as a critical residue for acetylation. We identified p300 and PCAF as two TRIM50 acetyltransferases and we further showed that a balance between ubiquitination and acetylation regulates TRIM50 degradation. |
| Databáze: | OpenAIRE |
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