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Børud B Hoang T Bakke M Jacob AL Lund J Mellgren G 《Molecular endocrinology (Baltimore, Md.)》2002,16(4):757-773
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Teyssier C Ou CY Khetchoumian K Losson R Stallcup MR 《Molecular endocrinology (Baltimore, Md.)》2006,20(6):1276-1286
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Watanabe M Yanagisawa J Kitagawa H Takeyama K Ogawa S Arao Y Suzawa M Kobayashi Y Yano T Yoshikawa H Masuhiro Y Kato S 《The EMBO journal》2001,20(6):1341-1352
One class of the nuclear receptor AF-2 coactivator complexes contains the SRC-1/TIF2 family, CBP/p300 and an RNA coactivator, SRA. We identified a subfamily of RNA-binding DEAD-box proteins (p72/p68) as a human estrogen receptor alpha (hER alpha) coactivator in the complex containing these factors. p72/p68 interacted with both the AD2 of any SRC-1/TIF2 family protein and the hER alpha A/B domain, but not with any other nuclear receptor tested. p72/p68, TIF2 (SRC-1) and SRA were co-immunoprecipitated with estrogen-bound hER alpha in MCF7 cells and in partially purified complexes associated with hER alpha from HeLa nuclear extracts. Estrogen induced co-localization of p72 with hER alpha and TIF2 in the nucleus. The presence of p72/p68 potentiated the estrogen-induced expression of the endogenous pS2 gene in MCF7 cells. In a transient expression assay, a combination of p72/p68 with SRA and one TIF2 brought an ultimate synergism to the estrogen-induced transactivation of hER alpha. These findings indicate that p72/p68 acts as an ER subtype-selective coactivator through ER alpha AF-1 by associating with the coactivator complex to bind its AF-2 through direct binding with SRA and the SRC-1/TIF2 family proteins. 相似文献
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Interaction of the tau2 transcriptional activation domain of glucocorticoid receptor with a novel steroid receptor coactivator, Hic-5, which localizes to both focal adhesions and the nuclear matrix 下载免费PDF全文
Yang L Guerrero J Hong H DeFranco DB Stallcup MR 《Molecular biology of the cell》2000,11(6):2007-2018