共查询到20条相似文献,搜索用时 31 毫秒
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Choi SM Choi KO Lee N Oh M Park H 《Biochemical and biophysical research communications》2006,343(4):1002-1008
The hypoxia-inducible factor-1alpha (HIF-1alpha) subunit is activated in response to lack of oxygen. HIF-1alpha-specific prolyl hydroxylase and factor inhibiting HIF-1alpha (FIH-1) catalyze hydroxylation of the proline and asparagine residues of HIF-1alpha, respectively. The hydroxyproline then interacts with ubiquitin E3 ligase, the von Hippel-Lindau protein, leading to degradation of HIF-1alpha by ubiquitin-dependent proteasomes, while the hydroxylation of the asparagine residue prevents recruitment of the coactivator, cAMP-response element-binding protein (CBP), thereby decreasing the transactivation ability of HIF-1alpha. We found that the Zn-specific chelator, N,N,N',N'-tetrakis (2-pyridylmethyl) ethylenediamine (TPEN), enhances the activity of HIF-1alpha-proline hydroxylase 2 but the level of HIF-1alpha protein does not fall because TPEN also inhibits ubiquitination. Since the Zn chelator does not prevent FIH-1 from hydroxylating the asparagine residue of HIF-1alpha, its presence leads to the accumulation of HIF-1alpha that is both prolyl and asparaginyl hydroxylated and is therefore nonfunctional. In hypoxic cells, TPEN also prevents HIF-1alpha from interacting with CBP, so reducing expression of HIF-1alpha target genes. As a result, Zn chelation causes the accumulation of nonfunctional HIF-1alpha protein in both normoxia and hypoxia. 相似文献
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Two transactivation mechanisms cooperate for the bulk of HIF-1-responsive gene expression 总被引:6,自引:0,他引:6
Kasper LH Boussouar F Boyd K Xu W Biesen M Rehg J Baudino TA Cleveland JL Brindle PK 《The EMBO journal》2005,24(22):3846-3858
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Activating signal cointegrator 1, a novel transcription coactivator of nuclear receptors, and its cytosolic localization under conditions of serum deprivation.
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Han-Jong Kim Ji-Young Yi Hee-Sook Sung David D. Moore Byung Hak Jhun Young Chul Lee Jae Woon Lee 《Molecular and cellular biology》1999,19(9):6323-6332
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Pereira T Zheng X Ruas JL Tanimoto K Poellinger L 《The Journal of biological chemistry》2003,278(9):6816-6823
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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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Molecular mechanisms of transcription activation by HLF and HIF1alpha in response to hypoxia: their stabilization and redox signal-induced interaction with CBP/p300 总被引:13,自引:0,他引:13
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Ema M Hirota K Mimura J Abe H Yodoi J Sogawa K Poellinger L Fujii-Kuriyama Y 《The EMBO journal》1999,18(7):1905-1914
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