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
HDAC6 mediates the acetylation of TRIM50 / Fusco, C; Micale, L; Augello, B; Mandriani, B; Pellico, Mt; De Nittis, P; Monti, Maria; Cozzolino, Flora; Pucci, Pietro; Merla, G.; Calcagnì, A. - In: CELLULAR SIGNALLING. - ISSN 0898-6568. - 26:2(2014), pp. 363-369. [10.1016/j.cellsig.2013.11.036]
HDAC6 mediates the acetylation of TRIM50
MONTI, MARIA;COZZOLINO, FLORA;PUCCI, PIETRO;Merla G.;
2014
Abstract
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| File | Dimensione | Formato | |
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HDAC6-TRIM50CellSignalling2014.pdf
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