| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| NA |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| In the case of ERbeta , phosphorylation enhances the ligand independent recruitment and action of SRC 1 . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Multivariate regression analyses were used to assess the relation between untreated cross sectional and longitudinal blood pressure and polymorphisms at the estrogen receptor alpha ( ESR 1 ) , estrogen receptor beta ( ESR 2 ) , aromatase ( CYP19A1 ) , and nuclear receptor coactivator 1 ( NCOA 1 ) genes after adjustment for common risk factors . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Surprisingly , the coactivator SRC 1 up regulates mER beta transactivation both in the absence and presence of E 2 , and in vitro interaction between SRC 1 and the ER beta ligand binding domain is enhanced by E 2 . ^^^ Moreover , the ligand independent stimulatory effect of SRC 1 on ER beta transcriptional activity is abolished by ICI 182 , 780 , but not by OHT . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| In addition , EM 652 blocks the E 2 dependent activation of ER alpha and ER beta by the steroid hormone receptor coactivator 1 as well as the in vitro interaction between SRC 1 and the ligand binding domains of both ERs . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| In affinity interaction assays for proteins that associate specifically with the hormone binding domain of these receptors , we demonstrate that the steroid receptor coactivator SRC 1 interacts in an estrogen dependent manner with ERalpha and ERbeta 1 , but not with ERbeta 2 . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| We demonstrate here that phosphorylation of AF 1 by MAP kinase ( MAPK ) leads to the recruitment of steroid receptor coactivator 1 ( SRC 1 ) by ER beta in vitro . ^^^ Enhancement of the interaction between SRC 1 and ER beta AF 1 is also observed in vivo in cells either treated with EGF or expressing activated Ras . ^^^ Two serine residues in ER beta AF 1 , of which one is contained within a motif present in other steroid receptors , are critical for physical interaction with SRC 1 and transcriptional activation . ^^^ Our results establish a role for nuclear receptor phosphorylation in the recruitment of SRC 1 and provide a molecular basis for ligand independent activation by ER beta via the MAPK pathway . . ^^^ Ligand independent recruitment of SRC 1 to estrogen receptor beta through phosphorylation of activation function AF 1 . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| EM 652 inhibits Ras induced transcriptional activity of ER alpha and ER beta and blocks SRC 1 stimulated activity of the two receptors . ^^^ EM 652 was also found to block the recruitment of SRC 1 at AF 1 of ER beta , this ligand independent activation of AF 1 being closely related to phosphorylation of the steroid receptors by protein kinase . ^^^ Most importantly , the antiestrogen hydroxytamoxifen has no inhibitory effect on the SRC 1 induced ER beta activity while the pure antiestrogen EM 652 completely abolishes this effect , thus strengthening the need to use pure antiestrogens in breast cancer therapy in order to control all known aspects of ER regulated gene expression . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| We used a fluorescent ligand for ER , tetrahydrochrysene ketone , to monitor the rates of ligand dissociation from ERalpha and ERbeta , and to see how this process is affected by the p 160 class coactivator , steroid receptor coactivator 1 ( SRC 1 ) . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| To obtain some clue to these roles , we screened the expression levels of ER alpha , ER beta , coactivators ( SRC 1 , TIF 2 , AIB 1 , CBP , and P / CAF ) and corepressors ( N CoR and SMRT ) in 6 normal mammary glands , 6 intraductal carcinomas , 22 invasive ductal carcinomas , and 7 breast cancer cell lines using a multiplex reverse transcription PCR . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Using a mammalian two hybrid assay , we show that the thyroid hormone receptor beta ( TRbeta ) and estrogen receptor beta ( ERbeta ) have different LXXLL motif preferences for interactions with SRC 1 . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| To investigate the molecular mechanisms underlying the ER subtype selective actions of these compounds , we have determined the conformational changes induced in ERalpha and ERbeta by these ligands using protease digestion sensitivity , and we have tested the ability of these ligands to promote the recruitment of representatives of the three SRC / p160 coactivator protein family members ( SRC 1 , GRIP 1 , ACTR , respectively ) to ERalpha and ERbeta using yeast two hybrid and glutathione S transferase ( GST ) pull down assays . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| We describe a ligand that binds to both receptors , but enhances only ER beta interaction with SRC 1 and SRC 3 while exhibiting little effect on the ER alpha interaction with these proteins . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Binding of ERbeta LBD to a coactivator peptide sequence containing the second LXXLL motif of steroid receptor coactivator 1 ( SRC 1 ( 2 ) ( 676 700 ) is shown to be specific and saturable . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Co transfections of coactivators such as SRC 1 , TIF 2 , AIB 1 , and TRAP 220 in 293T cells and use of the luciferase assay revealed that TRAP 220 failed to enhance the transcription mediated by ERbeta in the presence of ferutinine . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Employment of the human estrogen receptor beta ligand binding domain and co activator SRC 1 nuclear receptor binding domain for the construction of a yeast two hybrid detection system for endocrine disrupters . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| The interactions of human estrogen receptor subtypes ERalpha and ERbeta with DNA and a 210 amino acid residue fragment of the coactivator protein SRC 1 bearing three nuclear receptor interaction motifs were investigated quantitatively using fluorescence anisotropy in the presence of agonist and antagonist ligands . ^^^ Moreover , estrone and genistein exhibited subtype specificity in that they induced SRC 1 recruitment to ERbeta with much higher efficiency than in the case of ERalpha . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Furthermore , IA R bound ERalpha L384M and wild type ERbeta displayed enhanced interactions with the nuclear receptor interaction domains of the coactivators SRC 1 and GRIP 1 . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Interestingly , the overexpression of the steroid hormone receptor coactivator 1 ( SRC 1 ) resulted in preferential transcriptional enhancement by ERbeta as well as coexpressed ERalpha and ERbeta , whereas SRC 2 overexpression appeared to preferentially enhance ERalpha transactivation . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| The tumoral ER alpha protein expression was significantly correlated with that of PgR ( r = 0 . 61 , p = 0 . 001 ) and NCoR ( r = 0 . 4 , p = 0 . 043 ) , whereas ER beta expression was associated with SRC 1 ( r = 0 . 68 , p < or = . 001 ) , TIF 2 ( r = 0 . 64 , p = 0 . 001 ) and NCoR ( r = 0 . 48 , p = 0 . 014 ) protein levels in malignant specimens . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Both ER alpha and ER beta preferentially bound SRC 1 in the presence of beta estradiol . ^^^ Differential recruitment of SRC 1 and SMRT by ER alpha and ER beta in the presence of beta estradiol and 4 OHT may be central to the response of the tumor to endocrine treatment . . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Inverse relationship between ER beta and SRC 1 predicts outcome in endocrine resistant breast cancer . ^^^ To determine isoform specific expression of ER and coexpression with activator proteins , we examined the expression and localisation of ER alpha , ER beta and the coactivator protein steroid receptor coactivator 1 ( SRC 1 ) by immunohistochemistry and immunofluorescence in a cohort of human breast cancer patients ( n=150 ) . ^^^ Protein expression of ER beta and SRC 1 was inversely associated ( P=0 . 0001 ) . ^^^ The association of ER beta protein expression with increased DFS and its inverse relationship with SRC 1 suggests a role for these proteins in predicting outcome in breast cancer . . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| CHO K 1 cells transfected with ERalpha or ERbeta show ERE sequence dependent differences in the functional interaction of ERalpha and ERbeta with coactivators steroid receptor coactivator 1 ( SRC 1 ) , SRC 2 ( glucocorticoid receptor interacting protein 1 ( GRIP 1 ) ) , SRC 3 amplified in breast cancer 1 ( AIB 1 ) and ACTR , cyclic AMP binding protein ( CBP ) , and steroid receptor RNA activator ( SRA ) , corepressors nuclear receptor co repressor ( NCoR ) and silencing mediator for retinoid and thyroid hormone receptors ( SMRT ) , and secondary coactivators coactivator associated arginine methyltransferase 1 ( CARM 1 ) and protein arginine methyltransferase 1 ( PRMT 1 ) . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Ligand dependent estrogenic responses in NSCLC cells are probably generated via ERbeta and the p 160 coactivator GRIP1 / TIF2 , because expression of these proteins was detected , but not full length ERalpha or the p 160 coactivator SRC 1 . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Anisotropy measurements revealed that the affinity of this PGC 1alpha fragment for human ERalpha and beta was fairly strong in the presence of estradiol ( approximately 5 nM ) , and that unlike a similar fragment of SRC 1 ( 570 780 ) , PGC 191 408 exhibited ligand independent interactions with ER , particularly with ERbeta ( Kd approximately 30 nM ) . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| The repression in ERbeta response to hormone was dependent upon its AF 1 domain which includes serines 106 and 124 , two phosphorylation target sites for Erk that we previously showed to be involved in SRC 1 recruitment to ERbeta . ^^^ Moreover , expression of SRC 1 also relieved the inhibition of ERbeta in heregulin treated cells . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| The aim of the study was to test the hypothesis that expression of retinoid receptors ( RARalpha , RARbeta , RARgamma ) , rexinoid receptors ( RXRalpha , RXRbeta ) , thyroid hormone receptors ( TRalpha , TRbeta ) , estrogen receptors ( ERalpha , ERbeta ) , nuclear receptor coregulators ( N CoR , SRC 1 , SMRT ) , and in addition type 1 iodothyronine 5 ' deiodinase ( 5 ' DI ) , EGFR and erb B2 / neu would be different in mammary postlactating tissue in comparison with that of nonlactating mammary gland . ^^^ Using RT PCR , we have shown that expression of RARalpha , RXRalpha , TRalpha , ERalpha , ERbeta , N CoR , SRC 1 , SMRT and EGFR in rat was significantly increased in postlactating mammary gland when compared to that of nonlactating mammary tissue . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Sexually dimorphic expression of ER alpha and PR was noted with predominance in females and males , respectively , EE up regulating SRC 1 in males and ER beta and PR in females . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| In this work we have determined the role of the 26S proteasome in the regulation of the content of progesterone receptors ( PR A and PR B ) , estrogen receptors ( ER alpha and ER beta ) , the coactivator SRC 1 and the corepressor SMRT in the rat brain during the estrous cycle . ^^^ A significant increase in the content of both PR isoforms , ER beta and SRC 1 was observed after the administration of MG 132 in the three studied cerebral regions . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Herein , the molecular mechanisms involved in ER subtype selective interactions of these compounds as assessed by their effects upon both ERalpha and ERbeta structural conformation and their ability to induce recruitment of steroid receptor coactivator 1 ( SRC 1 ) to ERalpha were investigated . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Diffusional FCS data were obtained for a fluorescently labeled coactivator peptide , steroid receptor coactivator peptide 1 ( A SRC 1 ( 2 ) ) , in the absence and presence of bead bound ERbeta LBD . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Furthermore , hormone independent interaction of ERalpha and ERbeta mutant receptors with the steroid receptor coactivator 1 was abrogated by these antiestrogens . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Both ERalpha and ERbeta exhibited strong preferences for coactivator peptides corresponding to steroid receptor coactivator 1 and PPARgamma coactivor 1 vs . peroxisome proliferator activated receptor interacting protein and cAMP response element binding protein binding protein . 17beta Estradiol acted as a nonselective agonist for ERalpha and ERbeta . ^^^ |
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| Interacting proteins: Q15788 and Q92731 |
Pubmed |
SVM Score :0.0 |
| Coactivators steroid receptor coactivator 1 and cAMP response element binding protein binding protein synergistically activated hERalpha and ERbeta transcription and showed reduced efficacy with rERbeta and hERbeta1s , suggesting a role for the N terminus of ERbeta 1 in coactivator interaction . ^^^ |
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