Ontology highlight
ABSTRACT:
SUBMITTER: Faronato M
PROVIDER: S-EPMC3735711 | biostudies-literature | 2013 Jun
REPOSITORIES: biostudies-literature
Faronato Monica M Patel Vruti V Darling Sarah S Dearden Laura L Clague Michael J MJ Urbé Sylvie S Coulson Judy M JM
Cell cycle (Georgetown, Tex.) 20130520 12
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 polyubiquit ...[more]