Protein Aggregates Are Recruited to Aggresome by Histone Deacetylase 6 via Unanchored Ubiquitin C Termini*

@inproceedings{Ouyang2012ProteinAA,
  title={Protein Aggregates Are Recruited to Aggresome by Histone Deacetylase 6 via Unanchored Ubiquitin C Termini*},
  author={Hui Ouyang and Yousuf Omar Ali and Mani Ravichandran and Aiping Dong and Wei Qiu and F. Morell Mackenzie and Sirano dhe-Paganon and Cheryl H. Arrowsmith and R Grace Zhai},
  booktitle={The Journal of biological chemistry},
  year={2012}
}
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… CONTINUE READING
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