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Suh, Pann-Ghill
BioSignal Network Lab (BSN)
Research Interests
  • Signal transduction, cancer, metabolism, phospholipase C

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Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins

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Title
Activating signal cointegrator 2 belongs to a novel steady-state complex that contains a subset of trithorax group proteins
Author
Goo, YHSohn, YCKim, DHKim, SWKang, MJJung, DJKwak, EBarlev, NABerger, SLChow, VTRoeder, RGAzorsa, DOMeltzer, PSSuh, Pann-GhillSong, EJLee, KJLee, YCLee, JW
Issue Date
2003-01
Publisher
AMER SOC MICROBIOLOGY
Citation
MOLECULAR AND CELLULAR BIOLOGY, v.23, no.1, pp.140 - 149
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.
URI
https://scholarworks.unist.ac.kr/handle/201301/5613
URL
http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=0037216704
DOI
10.1128/MCB.23.1.140-149.2003
ISSN
0270-7306
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BIO_Journal Papers
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