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DC Field | Value | Language |
---|---|---|
dc.citation.endPage | 149 | - |
dc.citation.number | 1 | - |
dc.citation.startPage | 140 | - |
dc.citation.title | MOLECULAR AND CELLULAR BIOLOGY | - |
dc.citation.volume | 23 | - |
dc.contributor.author | Goo, YH | - |
dc.contributor.author | Sohn, YC | - |
dc.contributor.author | Kim, DH | - |
dc.contributor.author | Kim, SW | - |
dc.contributor.author | Kang, MJ | - |
dc.contributor.author | Jung, DJ | - |
dc.contributor.author | Kwak, E | - |
dc.contributor.author | Barlev, NA | - |
dc.contributor.author | Berger, SL | - |
dc.contributor.author | Chow, VT | - |
dc.contributor.author | Roeder, RG | - |
dc.contributor.author | Azorsa, DO | - |
dc.contributor.author | Meltzer, PS | - |
dc.contributor.author | Suh, Pann-Ghill | - |
dc.contributor.author | Song, EJ | - |
dc.contributor.author | Lee, KJ | - |
dc.contributor.author | Lee, YC | - |
dc.contributor.author | Lee, JW | - |
dc.date.accessioned | 2023-12-22T11:36:10Z | - |
dc.date.available | 2023-12-22T11:36:10Z | - |
dc.date.created | 2014-09-02 | - |
dc.date.issued | 2003-01 | - |
dc.description.abstract | Many transcription coactivators interact with nuclear receptors in a ligand- and C-terminal transactivation function (AF2)-dependent manner. These include activating signal cointegrator 2 (ASC-2), a recently isolated transcriptional coactivator molecule, which is amplified in human cancers and stimulates transactivation by nuclear receptors and numerous other transcription factors. In this report, we show that ASC-2 belongs to a steady-state complex of approximately 2 MDa (ASC-2 complex [ASCOM]) in HeLa nuclei. ASCOM contains retinoblastoma-binding protein RBQ-3, α/β-tubulins, and trithorax group proteins ALR-1, ALR-2, HALR, and ASH2. In particular, ALR-1/2 and HALR contain a highly conserved 130- to 140-amino-acid motif termed the SET domain, which was recently implicated in histone H3 lysine-specific methylation activities. Indeed, recombinant ALR-1, HALR, and immunopurified ASCOM exhibit very weak but specific H3-lysine 4 methylation activities in vitro, and transactivation by retinoic acid receptor appears to involve ligand-dependent recruitment of ASCOM and subsequent transient H3-lysine 4 methylation of the promoter region in vivo. Thus, ASCOM may represent a distinct coactivator complex of nuclear receptors. Further characterization of ASCOM will lead to a better understanding of how nuclear receptors and other transcription factors mediate transcriptional activation. | - |
dc.identifier.bibliographicCitation | MOLECULAR AND CELLULAR BIOLOGY, v.23, no.1, pp.140 - 149 | - |
dc.identifier.doi | 10.1128/MCB.23.1.140-149.2003 | - |
dc.identifier.issn | 0270-7306 | - |
dc.identifier.scopusid | 2-s2.0-0037216704 | - |
dc.identifier.uri | https://scholarworks.unist.ac.kr/handle/201301/5613 | - |
dc.identifier.url | http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037216704 | - |
dc.identifier.wosid | 000179970000013 | - |
dc.language | 영어 | - |
dc.publisher | AMER SOC MICROBIOLOGY | - |
dc.title | Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins | - |
dc.type | Article | - |
dc.description.journalRegisteredClass | scopus | - |
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