탈유비퀴틴화 효소 USP3에 의한 REST 단백질 안정성 조절에 관한 연구
- Title
- 탈유비퀴틴화 효소 USP3에 의한 REST 단백질 안정성 조절에 관한 연구
- Other Titles
- The protein stability of REST is regulated by deubiquitylase USP3
- Author
- 김민성
- Alternative Author(s)
- Min-Seong Kim
- Advisor(s)
- 김계성
- Issue Date
- 2017-08
- Publisher
- 한양대학교
- Degree
- Master
- 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.
- URI
- http://hdl.handle.net/20.500.11754/33838http://hanyang.dcollection.net/common/orgView/200000431680
- Appears in Collections:
- GRADUATE SCHOOL OF BIOMEDICAL SCIENCE AND ENGINEERING[S](의생명공학전문대학원) > BIOMEDICAL SCIENCE(의생명과학과) > Theses (Ph.D.)
- Files in This Item:
There are no files associated with this item.
- Export
- RIS (EndNote)
- XLS (Excel)
- XML