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://dcollection.hanyang.ac.kr/jsp/common/DcLoOrgPer.jsp?sItemId=000000102891http://hdl.handle.net/20.500.11754/33838
Appears in Collections:
GRADUATE SCHOOL OF BIOMEDICAL SCIENCE AND ENGINEERING[S](의생명공학전문대학원) > BIOMEDICAL SCIENCE(의생명과학과) > Theses (Ph.D.)
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