The deubiquitylase USP15 stabilizes newly synthesized REST and rescues its expression at mitotic exit

@inproceedings{Faronato2013TheDU,
  title={The deubiquitylase USP15 stabilizes newly synthesized REST and rescues its expression at mitotic exit},
  author={Monica Faronato and Vruti Patel and Sarah Darling and Laura Dearden and Michael J Clague and Sylvie Urb{\'e} and Judy M Coulson},
  booktitle={Cell cycle},
  year={2013}
}
Reversible ubiquitylation of proteins contributes to their integrity, abundance and activity. The RE1-silencing transcription factor (REST) plays key physiological roles and is dysregulated in a spectrum of disease. It is rapidly turned over and is phosphorylated, polyubiquitylated and degraded en masse during neuronal differentiation and cell cycle progression. Through siRNA screening we identified the deubiquitylase USP15 as a key regulator of cellular REST. Both antagonism of REST… CONTINUE READING
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