HDAC6 mediates the acetylation of TRIM50

Carmela Fusco, Lucia Micale, Bartolomeo Augello, Barbara Mandriani, Maria Teresa Pellico, Pasquelena De Nittis, Alessia Calcagnì, Maria Monti, Flora Cozzolino, Piero Pucci, Giuseppe Merla

Research output: Contribution to journalArticle

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.

Original languageEnglish
Pages (from-to)363-369
Number of pages7
JournalCellular Signalling
Volume26
Issue number2
DOIs
Publication statusPublished - Feb 2014

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Keywords

  • Acetylation
  • HDAC6
  • NES
  • TRIM50
  • Ubiquitination

ASJC Scopus subject areas

  • Cell Biology

Cite this

Fusco, C., Micale, L., Augello, B., Mandriani, B., Pellico, M. T., De Nittis, P., Calcagnì, A., Monti, M., Cozzolino, F., Pucci, P., & Merla, G. (2014). HDAC6 mediates the acetylation of TRIM50. Cellular Signalling, 26(2), 363-369. https://doi.org/10.1016/j.cellsig.2013.11.036