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Modification of CHFR by O-linked N-acetylglucosamine regulates its stability : O-linked N-acetylglucosamine modification에 의한 CHFR의 활성 조절에 관한 연구
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- Authors
- Advisor
- 설재홍
- Major
- 자연과학대학 생명과학부
- Issue Date
- 2013-08
- Publisher
- 서울대학교 대학원
- Keywords
- CHFR ; Tumor suppressor ; O-GlcNAcylation ; OGT ; OGA
- Description
- 학위논문 (석사)-- 서울대학교 대학원 : 생명과학부, 2013. 8. 설재홍.
- Abstract
- O-linked β-N-acetylglucosamine (O-GlcNAc) modification (O-GlcNAcylation) of proteins is important for modulating many cellular processes such as signal transduction, transcription, translation and proteasomal degradation. Only two enzymes are known to regulate O-GlcNAcylation in mammals: O-GlcNAc transferase (OGT) and O-GlcNAcase (OGA).
CHFR tumor suppressor is a checkpoint protein that delays cell cycle progression upon DNA damage. Moreover, CHFR ubiquitinates key mitotic kinases such as Aurora A and PLK1 leading to their degradation by proteasomes. Althrough the significance role in the control of cell growth, little is known on how CHFR activity is regulated.
Here, i showed that tumor suppressor CHFR was modified with O-GlcNAc. Moreover, the levels of O-GlcNAcylated CHFR increased when overexpressed OGT and/or OGA was blocked by Thiamet G, an O-GlcNAcase inhibitor. And CHFR was modified with O-GlcNAc at Ser164 and Ser165, analysed by mass spectrometry. I confirmed that O-GlcNAcylation of CHFR positively regulates its stability. Thus, O-GlcNAcylation may contribute a new regulatory mechanism of CHFR.
- Language
- English
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