There are no files associated with this item.
Full metadata record
DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 887 | - |
dc.citation.number | 4 | - |
dc.citation.startPage | 881 | - |
dc.citation.title | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | - |
dc.citation.volume | 470 | - |
dc.contributor.author | Park, I. Seul | - |
dc.contributor.author | Han, Ye Gi | - |
dc.contributor.author | Chung, Hee Jin | - |
dc.contributor.author | Jung, Yong Woo | - |
dc.contributor.author | Kim, Yonghwan | - |
dc.contributor.author | Kim, Hongtae | - |
dc.date.accessioned | 2023-12-22T00:08:53Z | - |
dc.date.available | 2023-12-22T00:08:53Z | - |
dc.date.created | 2018-09-19 | - |
dc.date.issued | 2016-02 | - |
dc.description.abstract | TRAIP/RNF206 plays diverse roles in cell cycle progression, DNA damage response, and DNA repair pathways. Physiological importance of TRAIP is highlighted by the identification of pathogenic mutations of TRAIP gene in patients diagnosed with primordial dwarfism. Although the diverse functions of TRAIP in the nucleus have been well characterized, molecular mechanism of TRAIP retention in the nucleus has not been determined. Here, we discovered that TRAIP is post-translationally modified by the small ubiquitin-like protein (SUMO). In addition, we identified five SUMOylation sites in TRAIP, and successfully generated SUMOylation deficient mutant of TRAIP. In an attempt to define the functional roles of TRAIP SUMOylation, we discovered that SUMOylation deficient TRAIP is not retained in the nucleus. In addition, protein stability of SUMOylation deficient TRAIP is lower than wild type TRAIP, demonstrating that SUMOylation is critical for both proper subcellular localization and protein stability of TRAIP. Taken together, these findings improve the understanding clinical implication of TRAIP in various diseases including primordial dwarfism and cancers. | - |
dc.identifier.bibliographicCitation | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, v.470, no.4, pp.881 - 887 | - |
dc.identifier.doi | 10.1016/j.bbrc.2016.01.141 | - |
dc.identifier.issn | 0006-291X | - |
dc.identifier.scopusid | 2-s2.0-84957428501 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/24881 | - |
dc.identifier.url | https://www.sciencedirect.com/science/article/pii/S0006291X16301425?via%3Dihub | - |
dc.identifier.wosid | 000370582300017 | - |
dc.language | 영어 | - |
dc.publisher | ACADEMIC PRESS INC ELSEVIER SCIENCE | - |
dc.title | SUMOylation regulates nuclear localization and stability of TRAIP/RNF206 | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.subject.keywordAuthor | TRAIP | - |
dc.subject.keywordAuthor | SUMOylation | - |
dc.subject.keywordAuthor | Subcellular localization | - |
dc.subject.keywordAuthor | Protein degradation | - |
dc.subject.keywordPlus | INTERACTING PROTEIN TRIP | - |
dc.subject.keywordPlus | TUMOR-NECROSIS-FACTOR | - |
dc.subject.keywordPlus | KAPPA-B ACTIVATION | - |
dc.subject.keywordPlus | DNA-DAMAGE | - |
dc.subject.keywordPlus | RAP80 | - |
dc.subject.keywordPlus | DEGRADATION | - |
dc.subject.keywordPlus | COMPONENT | - |
dc.subject.keywordPlus | PROMOTES | - |
dc.subject.keywordPlus | TRAIP | - |
dc.subject.keywordPlus | PIAS1 | - |
Items in Repository are protected by copyright, with all rights reserved, unless otherwise indicated.
Tel : 052-217-1404 / Email : scholarworks@unist.ac.kr
Copyright (c) 2023 by UNIST LIBRARY. All rights reserved.
ScholarWorks@UNIST was established as an OAK Project for the National Library of Korea.