[HTML][HTML] Protein aggregates are recruited to aggresome by histone deacetylase 6 via unanchored ubiquitin C termini
H Ouyang, YO Ali, M Ravichandran, A Dong… - Journal of Biological …, 2012 - ASBMB
The aggresome pathway is activated when proteasomal clearance of misfolded proteins is
hindered. Misfolded polyubiquitinated protein aggregates are recruited and transported to
the aggresome via the microtubule network by a protein complex consisting of histone
deacetylase 6 (HDAC6) and the dynein motor complex. The current model suggests that
HDAC6 recognizes protein aggregates by binding directly to polyubiquitinated proteins.
Here, we show that there are substantial amounts of unanchored ubiquitin in protein …
hindered. Misfolded polyubiquitinated protein aggregates are recruited and transported to
the aggresome via the microtubule network by a protein complex consisting of histone
deacetylase 6 (HDAC6) and the dynein motor complex. The current model suggests that
HDAC6 recognizes protein aggregates by binding directly to polyubiquitinated proteins.
Here, we show that there are substantial amounts of unanchored ubiquitin in protein …