DC Field | Value | Language |
---|---|---|
dc.contributor.advisor | Kim, Seyun | - |
dc.contributor.advisor | 김세윤 | - |
dc.contributor.author | Park, Jeong Eun | - |
dc.date.accessioned | 2019-09-03T02:42:38Z | - |
dc.date.available | 2019-09-03T02:42:38Z | - |
dc.date.issued | 2018 | - |
dc.identifier.uri | http://library.kaist.ac.kr/search/detail/view.do?bibCtrlNo=733865&flag=dissertation | en_US |
dc.identifier.uri | http://hdl.handle.net/10203/266274 | - |
dc.description | 학위논문(석사) - 한국과학기술원 : 생명과학과, 2018.2,[ii, 34 p. :] | - |
dc.description.abstract | IPMK is a versatile protein exhibiting catalytic and non-catalytic activities, acting as a signaling hub in the biological pathways. p62, also known as sequestosome-1, is a scaffold protein in signal transduction by interacting with critical signaling intermediates. In this study, I showed that IPMK and p62 physically interact each other. Deficiency of IPMK did not affect autophagy, a cellular degradation system in which p62 known to act as an adaptor. Interestingly, IPMK and p62 in cultured macrophages were dynamically recruited to each other in response to palmitate, which induces TLR4 signaling. Taken together, this study reveals the presence of IPMK-p62 interaction through a direct binding and suggests that this interaction of the two signaling proteins may have a significant role in signal transduction. | - |
dc.language | eng | - |
dc.publisher | 한국과학기술원 | - |
dc.subject | Inositol polyphosphate multikinase▼ap62/Sequestosome-1▼asignal transduction▼ainteraction▼ainflammation | - |
dc.subject | 이노시톨 다인산 멀티키나아제▼a유비퀴틴 결합 단백질▼a신호전달▼a상호 작용▼a염증 반응 | - |
dc.title | Characterization of the Molecular Interaction between Inositol Polyphosphate Multikinase and p62/SQSTM1 | - |
dc.title.alternative | 이노시톨 다인산 멀티키나아제와 p62/SQSTM1 간 분자적 상호결합 규명 연구 | - |
dc.type | Thesis(Master) | - |
dc.identifier.CNRN | 325007 | - |
dc.description.department | 한국과학기술원 :생명과학과, | - |
dc.contributor.alternativeauthor | 박정은 | - |
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.