RETRACTED: Nuclear receptor function requires a TFTC-type histone acetyl transferase complex (Retracted article. See vol. 54, pg. 536, 2014)

被引:137
作者
Yanagisawa, J
Kitagawa, H
Yanagida, M
Wada, O
Ogawa, S
Nakagomi, M
Oishi, H
Yamamoto, Y
Nagasawa, H
McMahon, SB
Cole, MD
Tora, L
Takahashi, N
Kato, S [1 ]
机构
[1] Univ Tokyo, Grad Sch Agr & Life Sci, Inst Mol & Cellular Biosci, Bunkyo Ku, Tokyo 1130032, Japan
[2] Univ Tokyo, Grad Sch Agr & Life Sci, Dept Appl Biol Chem, Bunkyo Ku, Tokyo 1130032, Japan
[3] Univ Agr & Technol, Dept Appl Biol Sci, Fuchu, Tokyo 1838509, Japan
[4] Princeton Univ, Dept Biol Mol, Princeton, NJ 08544 USA
[5] ULP, INSERM, CNRS, Inst Genet & Biol Mol & Cellulaire, F-67404 Illkirch Graffenstaden, France
[6] CU Strasbourg, Strasbourg, France
[7] Japan Sci & Technol, CREST, Kawaguchi, Saitama 3320012, Japan
关键词
D O I
10.1016/S1097-2765(02)00478-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Nuclear receptors (NRs) regulate transcription in a [ligand-dependent way through two types of coactivator complexes: the p160/CBP histone acetyl transferase (HAT) complex and the DRIP/TRAP/SMCC complex without HAT activity. Here we identified a large human (h) coactivator complex necessary for the estrogen receptor alpha (ERalpha) transactivation. This complex contains the GCN5 HAT, the c-Myc interacting protein TRRAP/PAF400, TAF1130, and other subunits. Similarly to known TFTC (TBP-free TAFII-containing)-type HAT complexes (hTFTC, hPCAF, and hSTAGA), TRRP directly interacted with liganded ERalpha, or other NRs. ERalpha transactivation was enhanced by the purified complex in vitro. Antisense TRRAP RNA inhibited estrogendependent cell growth of breast cancer cells. Thus, the isolated TFTC-type HAT complex acts as a third class of coactivator complex for NR function.
引用
收藏
页码:553 / 562
页数:10
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