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Steroid receptor coactivator 1 links the steroid and interferon gamma response pathways 总被引:2,自引:0,他引:2
Tzortzakaki E Spilianakis C Zika E Kretsovali A Papamatheakis J 《Molecular endocrinology (Baltimore, Md.)》2003,17(12):2509-2518
We show here that steroid receptor coactivator 1 (SRC-1) is a coactivator of MHC class II genes that stimulates their interferon gamma (IFNgamma) and class II transactivator (CIITA)-mediated expression. SRC-1 interacts physically with the N-terminal activation domain of CIITA through two regions: one central [extending from amino acids (aa) 360-839] that contains the nuclear receptors binding region and one C-terminal (aa 1138-1441) that contains the activation domain 2. Using chromatin immunoprecipitation assays we show that SRC-1 recruitment on the class II promoter is enhanced upon IFNgamma stimulation. Most importantly, SRC-1 relieves the inhibitory action of estrogens on the IFNgamma-mediated induction of class II genes in transient transfection assays. We provide evidence that inhibition by estradiol is due to multiple events such as slightly reduced recruitment of CIITA and SRC-1 and severely inhibited assembly of the preinitiation complex. 相似文献
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Oh AS Lahusen JT Chien CD Fereshteh MP Zhang X Dakshanamurthy S Xu J Kagan BL Wellstein A Riegel AT 《Molecular and cellular biology》2008,28(21):6580-6593
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JAB1 interacts with both the progesterone receptor and SRC-1 总被引:8,自引:0,他引:8
Chauchereau A Georgiakaki M Perrin-Wolff M Milgrom E Loosfelt H 《The Journal of biological chemistry》2000,275(12):8540-8548
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SRC-3/AIB1 is a steroid receptor coactivator with potent growth-promoting activity, and its overexpression is sufficient to induce tumorigenesis. Previous studies indicate that the cellular level of SRC-3 is tightly regulated by both ubiquitin-dependent and ubiquitin-independent proteasomal degradation pathways. Atypical protein kinase C (aPKC) is frequently overexpressed in cancers. In the present study, we show that aPKC phosphorylates and specifically stabilizes SRC-3 in a selective ER-dependent manner. We further demonstrate that an acidic residue-rich region in SRC-3 is an important determinant for aPKC-mediated phosphorylation and stabilization. The mechanism of the aPKC-mediated stabilization appears due to a decreased interaction between SRC-3 and the C8 subunit of the 20S core proteasome, thus preventing SRC-3 degradation. Our results demonstrate a potent signaling mechanism for regulating SRC-3 levels in cells by coordinate enzymatic inhibition of both ubiquitin-dependent and ubiquitin-independent proteolytic pathways. 相似文献
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