탈유비퀴틴화 효소 USP3에 의한 REST 단백질 안정성 조절에 관한 연구

Abstract

The repressor element 1-silencing transcription factor (REST) gene encodes a transcriptional repressor that represses neuronal genes in non-neuronal tissues. The protein is also found in undifferentiated neuronal progenitor cells and this repressor might act as a master negative regular of neurogenesis. Information regarding the post-translational modifications (PTM) of REST protein stability and function is limited. Therefore, in this study, we explored deubiquitination of REST protein and its subsequent stability by Ubiquitin-specific protease 3 (USP3). USP3 is a deubiquitinating enzyme which interacts, deubiquitinates and stabilizes REST protein by prolonging its half-life and by reversing its proteasomal turnover. Herein, we report role of USP3 via PTM based regulation of REST protein. We further suggest the need to validate the potential effect of USP3 in promoting the maintenance of neural progenitor cells.