共查询到20条相似文献,搜索用时 640 毫秒
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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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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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Identification of protein arginine methyltransferase 2 as a coactivator for estrogen receptor alpha 总被引:1,自引:0,他引:1
Qi C Chang J Zhu Y Yeldandi AV Rao SM Zhu YJ 《The Journal of biological chemistry》2002,277(32):28624-28630
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Amanda Rui En Woo Siu Kwan Sze Hwa Hwa Chung Valerie C-L Lin 《Biochimica et Biophysica Acta (BBA) - Gene Regulatory Mechanisms》2019,1862(4):522-533
The activation functions AF1 and AF2 of nuclear receptors mediate the recruitment of coregulators in gene regulation. AF1 is mapped to the highly variable and intrinsically unstructured N terminal domain and AF2 lies in the conserved ligand binding domain. The unstructured nature of AF1 offers structural plasticity and hence functional versatility in gene regulation. However, little is known about the key functional residues of AF1 that mediates its interaction with coregulators. This study focuses on the progesterone receptor (PR) and reports the identification of K464, K481 and R492 (KKR) as the key functional residues of PR AF1. The KKR are monomethylated and function cooperatively. The combined mutations of KKR to QQQ render PR isoform B (PRB) hyperactive, whereas KKR to FFF mutations abolishes as much as 80% of PR activity. Furthermore, the hyperactive QQQ mutation rescues the loss of PR activity due to E911A mutation in AF2. The study also finds that the magnitudes of the mutational effect differ in different cell types as a result of differential effects on the functional interaction with coregulators. Furthermore, KKR provides the interface for AF1 to physically interact with p300 and SRC-1, and with AF2 at E911. Intriguingly, the inactive FFF mutant interacts strikingly stronger with both SRC-1 and AF2 than wt PRB. We propose a tripartite model to describe the dynamic interactions between AF1, AF2 and SRC-1 with KKR of AF1 and E911 of AF2 as the interface. An overly stable interaction would hamper the dynamics of disassembly of the receptor complex. 相似文献
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Peptidyl-prolyl isomerase 1 (Pin1) serves as a coactivator of steroid receptor by regulating the activity of phosphorylated steroid receptor coactivator 3 (SRC-3/AIB1) 总被引:4,自引:0,他引:4
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Yi P Wu RC Sandquist J Wong J Tsai SY Tsai MJ Means AR O'Malley BW 《Molecular and cellular biology》2005,25(21):9687-9699