Histone deacetylase 3 is selectively involved in L3MBTL2-mediated transcriptional repression
DC Field | Value | Language |
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dc.contributor.author | Yoo, Jung-Yoon | - |
dc.contributor.author | Choi, Kyung-Chul | - |
dc.contributor.author | Kang, HeeBum | - |
dc.contributor.author | Kim, Young Jun | - |
dc.contributor.author | Lee, Jeongmin | - |
dc.contributor.author | Jun, Woo Jin | - |
dc.contributor.author | Kim, Mi-Jeong | - |
dc.contributor.author | Lee, Yoo-Hyun | - |
dc.contributor.author | Lee, Ok-Hee | - |
dc.contributor.author | Yoon, Ho-Geun | - |
dc.date.accessioned | 2021-09-08T02:30:10Z | - |
dc.date.available | 2021-09-08T02:30:10Z | - |
dc.date.created | 2021-06-11 | - |
dc.date.issued | 2010-06-03 | - |
dc.identifier.issn | 0014-5793 | - |
dc.identifier.uri | https://scholar.korea.ac.kr/handle/2021.sw.korea/116260 | - |
dc.description.abstract | This is the first report that L(3) mbt-like 2 (L3MBTL2) specifically interacts with the histone deacetylase domain of histone deacetylase 3 (HDAC3) via its MBT domain. Here, we show that L3MBTL2 selectively interacts with HDAC3, but not other class I HDACs. An in vitro peptide-binding assay demonstrated the specific association of HDAC3 with methylated histone-K20 tail and L3MBTL2. Furthermore, depletion of HDAC3 resulted in a decrease of methylated K20-H4, as well as an increase in acetylated histone H3. Consequently, HDAC3 knock-down selectively suppressed L3MBTL2-mediated transcriptional repression. Taken together, our results reveal the concerted action of both HDAC3 and L3MBTL2 in histone deacetylation and methylation-dependent transcriptional repression. Structured summary: MINT-7719975: L3MBTL2 (uniprotkb:Q969R5) and HDAC3 (uniprotkb:O15379) colocalize (MI:0403) by fluorescence microscopy (MI: 0416) MINT-7719941, MINT-7719921: L3MBTL2 (uniprotkb: Q969R5) binds (MI: 0407) to HDAC3 (uniprotkb: O15379) by pull down (MI: 0096) MINT-7719991: HDAC3 (uniprotkb: O15379) physically interacts (MI: 0915) with L3MBTL2 (uniprotkb: Q969R5) by anti bait coimmunoprecipitation (MI: 0006) MINT-7719958: L3MBTL2 (uniprotkb: Q969R5) physically interacts (MI: 0915) with HDAC3 (uniprotkb: O15379) by anti tag coimmunoprecipitation (MI: 0007) MINT-7719897: HDAC3 (uniprotkb: O15379) physically interacts (MI: 0915) with L3MBTL2 (uniprotkb: Q969R5) by two hybrid (MI: 0018) (C) 2010 Federation of European Biochemical Societies. Published by Elsevier B. V. All rights reserved. | - |
dc.language | English | - |
dc.language.iso | en | - |
dc.publisher | ELSEVIER SCIENCE BV | - |
dc.subject | L3MBTL1 | - |
dc.subject | COMPLEX | - |
dc.title | Histone deacetylase 3 is selectively involved in L3MBTL2-mediated transcriptional repression | - |
dc.type | Article | - |
dc.contributor.affiliatedAuthor | Kim, Young Jun | - |
dc.identifier.doi | 10.1016/j.febslet.2010.03.048 | - |
dc.identifier.scopusid | 2-s2.0-77952953188 | - |
dc.identifier.wosid | 000277793200009 | - |
dc.identifier.bibliographicCitation | FEBS LETTERS, v.584, no.11, pp.2225 - 2230 | - |
dc.relation.isPartOf | FEBS LETTERS | - |
dc.citation.title | FEBS LETTERS | - |
dc.citation.volume | 584 | - |
dc.citation.number | 11 | - |
dc.citation.startPage | 2225 | - |
dc.citation.endPage | 2230 | - |
dc.type.rims | ART | - |
dc.type.docType | Article | - |
dc.description.journalClass | 1 | - |
dc.description.journalRegisteredClass | scie | - |
dc.description.journalRegisteredClass | scopus | - |
dc.relation.journalResearchArea | Biochemistry & Molecular Biology | - |
dc.relation.journalResearchArea | Biophysics | - |
dc.relation.journalResearchArea | Cell Biology | - |
dc.relation.journalWebOfScienceCategory | Biochemistry & Molecular Biology | - |
dc.relation.journalWebOfScienceCategory | Biophysics | - |
dc.relation.journalWebOfScienceCategory | Cell Biology | - |
dc.subject.keywordPlus | L3MBTL1 | - |
dc.subject.keywordPlus | COMPLEX | - |
dc.subject.keywordAuthor | L(3)mbt-like 2 | - |
dc.subject.keywordAuthor | Histone deacetylase 3 | - |
dc.subject.keywordAuthor | MBT domain | - |
dc.subject.keywordAuthor | Transcription | - |
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