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Sohn, Young Chang,Goo, Young-Wha,Kim, Dae-Hwan,Kim, Seung-Whan,Kang, Min-Jung,Nickolai A. Barlev,Shelley L. Berger,Vincent T. Chow,Suh, Pan-Gil,David O. Azorsa,Paul S. Meltzer,Lee, Kong-Ju,Lee, Young- 이화여자대학교 세포신호전달연구센터 2002 고사리 세포신호전달 심포지움 Vol. No.4
Activating signal cointegrator-2(ASC-2), also reported as AIB3, TRBP, RAP250, NRC and PRIP, directly binds to and functions as a coactivator molecule of nuclear receptors and many other transcription factors. In particular, our previous results from microinjection of anti-ASC2 antibody demonstrated that ASC-2 is required for transactivation by nuclear receptors and AP-1 in vivo. Here we show that ASC-2 belongs to a steady-state complex of approximately 2 MDa(ASCOM for ASC-2 complex) in HeLa nuclei, which contains mammalian homologues of Drosophila Trithorax group(Trx-G) proteins ALR-1, ALR-2, HALR and ASH2. ALR-1/2 and HALR contain a SET domain that specifically methylates histone H3 lysine 4(K4). We further demonstrate that retinoic acid receptor(RAR) transactivation requires retinoid-dependent recruitment of ASCOM to DNA-bound RAR in vivo. Thus, ASCOM represents the first mammalian coactivator complex with H3/K4-methylase activity, directly recruited to nuclear receptors.