Cited 0 times in
Diverse biological functions of HDAC3 corepressor complexes
DC Field | Value | Language |
---|---|---|
dc.contributor.author | 최경철 | - |
dc.date.accessioned | 2015-11-21T07:48:25Z | - |
dc.date.available | 2015-11-21T07:48:25Z | - |
dc.date.issued | 2010 | - |
dc.identifier.uri | https://ir.ymlib.yonsei.ac.kr/handle/22282913/125170 | - |
dc.description | 의과학과/박사 | - |
dc.description.abstract | [한글] [영문]The reversible acetylation by HDAC and HAT is known to be crucial for the stability of p53 and p53-dependent apoptotic signaling. To unravel the functional significance of HDAC3 involved in apoptosis, the yeast-two hybrid assay was performed, and finally identified the proapototic protein, PDCD5 as a novel-HDAC3 interacting protein. Diverse protein-protein interacting analysis found that PDCD5 selectively interacts with HDAC3 among class I HDACs. This study shows that PDCD5-mediated HDAC3 cleavage upon apoptotic stress is dependent on caspase-3. Depletion of either PDCD5 or caspase-3 failed to induce the HDAC3-cleavage and diverse apototic event, indicating that PDCD5-capspase-3 cascade is generally essential for apoptosis. Furthermore, PDCD3-caspase-3 complex directly mediates the ectoposide-induced HDAC3 cleavage and reduction of histone deacetylase activity, and finally increase of cytoplasmic accumulation of HDAC3. More importantly, caspase-3-dependent HDAC3 cleavage by PDCD5 act as a modulator for the maintenance of p53 acetylation and stability. | - |
dc.description.statementOfResponsibility | prohibition | - |
dc.publisher | 연세대학교 대학원 | - |
dc.rights | CC BY-NC-ND 2.0 KR | - |
dc.rights.uri | https://creativecommons.org/licenses/by-nc-nd/2.0/kr/ | - |
dc.title | Diverse biological functions of HDAC3 corepressor complexes | - |
dc.title.alternative | HDAC3 전사억제자 복합체들의 다양한 생물학적 기능 규명 | - |
dc.type | Thesis | - |
dc.contributor.alternativeName | Choi, Kyung Chul | - |
dc.type.local | Dissertation | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.