HDAC6 mediates the acetylation of TRIM50

Cell Signal. 2014 Feb;26(2):363-9. doi: 10.1016/j.cellsig.2013.11.036. Epub 2013 Dec 2.

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.

Keywords: Acetylation; HDAC6; NES; TRIM50; Ubiquitination.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Animals
  • Cell Line
  • HEK293 Cells
  • HeLa Cells
  • Histone Deacetylase 6
  • Histone Deacetylases / genetics
  • Histone Deacetylases / metabolism*
  • Humans
  • Mice
  • Microtubules / metabolism
  • Protein Binding
  • Protein Structure, Tertiary
  • Tripartite Motif Proteins
  • Ubiquitin-Protein Ligases / chemistry
  • Ubiquitin-Protein Ligases / metabolism*
  • Ubiquitination
  • p300-CBP Transcription Factors / metabolism

Substances

  • Tripartite Motif Proteins
  • p300-CBP Transcription Factors
  • p300-CBP-associated factor
  • TRIM50 protein, human
  • Ubiquitin-Protein Ligases
  • HDAC6 protein, human
  • Histone Deacetylase 6
  • Histone Deacetylases