scholarly journals Vitamin D-interacting Protein 205 (DRIP205) Coactivation of Estrogen Receptor α (ERα) Involves Multiple Domains of Both Proteins

2004 ◽  
Vol 279 (51) ◽  
pp. 53602-53612 ◽  
Author(s):  
Qian Wu ◽  
Robert Burghardt ◽  
Stephen Safe
Keyword(s):  
Vitamin D ◽  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Interacting Protein ◽  
Multiple Domains

scholarly journals Novel CARM1-Interacting Protein, DZIP3, Is a Transcriptional Coactivator of Estrogen Receptor-α

2015 ◽  
Vol 29 (12) ◽  
pp. 1708-1719 ◽  
Author(s):  
Daniel J. Purcell ◽  
Swati Chauhan ◽  
Diane Jimenez-Stinson ◽  
Kathleen R. Elliott ◽  
Tenzin D. Tsewang ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Transcriptional Coactivator ◽  
Interacting Protein

scholarly journals Transrepression of the estrogen receptor promoter by calcitriol in human breast cancer cells via two negative vitamin D response elements

2013 ◽  
Vol 20 (4) ◽  
pp. 565-577 ◽  
Author(s):  
Srilatha Swami ◽  
Aruna V Krishnan ◽  
Lihong Peng ◽  
Johan Lundqvist ◽  
David Feldman
Keyword(s):  
Breast Cancer ◽  
Vitamin D ◽  
Estrogen Receptor ◽  
Promoter Sequence ◽  
Estrogen Receptor Α ◽  
Mobility Shift ◽  
Response Elements ◽  
Dihydroxyvitamin D ◽  
Mobility Shift Assay ◽  
Estrogen Receptor Promoter

Calcitriol (1,25-dihydroxyvitamin D3), the hormonally active metabolite of vitamin D, exerts its anti-proliferative activity in breast cancer (BCa) cells by multiple mechanisms including the downregulation of the expression of estrogen receptor α (ER). We analyzed an ∼3.5 kb ER promoter sequence and demonstrated the presence of two potential negative vitamin D response elements (nVDREs), a newly identified putative nVDRE upstream at −2488 to −2473 bp (distal nVDRE) and a previously published sequence (proximal nVDRE) at −94 to −70 bp proximal to the P1 start site. Transactivation analysis using ER promoter deletion constructs and heterologous promoter–reporter constructs revealed that both nVDREs functioned to mediate calcitriol transrepression. In the electrophoretic mobility shift assay, the vitamin D receptor (VDR) showed strong binding to both nVDREs in the presence of calcitriol, and the chromatin immunoprecipitation assay demonstrated the recruitment of the VDR to the distal nVDRE site. Mutations in the 5′ hexameric DNA sequence of the distal nVDRE resulted in the loss of calcitriol-mediated transrepression and the inhibition of protein–DNA complex formation, demonstrating the importance of these nucleotides in VDR DNA binding and transrepression. A putative nuclear factor-Y (NFY) binding site, identified within the distal nVDRE, led to the findings that NFY bound to the distal nVDRE site interfered with the binding of the VDR at the site and reduced calcitriol-mediated transrepression. In conclusion, the ER promoter region contains two negative VDREs that act in concert to bind to the VDR and both nVDREs are required for the maximal inhibition of ER expression by calcitriol. The suppression of ER expression and estrogen-mediated signaling by calcitriol in BCa cells suggests that vitamin D may be useful in the treatment of ER+ BCa.

Vitamin D and estrogen receptor-α genotype and indices of bone mass and bone turnover in Danish girls

2006 ◽  
Vol 24 (4) ◽  
pp. 329-336 ◽  
Author(s):  
Siobhan Cusack ◽  
Christian Mølgaard ◽  
Kim F. Michaelsen ◽  
Jette Jakobsen ◽  
Christel J.E. Lamberg-Allardt ◽  
...  
Keyword(s):  
Vitamin D ◽  
Estrogen Receptor ◽  
Bone Mass ◽  
Bone Turnover ◽  
Estrogen Receptor Α

scholarly journals Phosphorylation of Estrogen Receptor α at Serine 118 Directs Recruitment of Promoter Complexes and Gene-Specific Transcription

Endocrinology ◽  
2011 ◽  
Vol 152 (6) ◽  
pp. 2517-2526 ◽  
Author(s):  
Tamika T. Duplessis ◽  
Christopher C. Williams ◽  
Steven M. Hill ◽  
Brian G. Rowan
Keyword(s):  
Estrogen Receptor ◽  
Cyclin D1 ◽  
Transcriptional Activation ◽  
Protein Complexes ◽  
Estrogen Receptor Α ◽  
Gene Promoters ◽  
Interacting Protein ◽  
Steroid Receptor Coactivator ◽  
Estrogen Response ◽  
Transcriptional Coregulators

Phosphorylation of estrogen receptor α (ERα) is important for receptor function, although the role of specific ERα phosphorylation sites in ERα-mediated transcription remains to be fully evaluated. Transcriptional activation by ERα involves dynamic, coordinate interactions with coregulators at promoter enhancer elements to effect gene expression. To determine whether ERα phosphorylation affects recruitment of unique protein complexes at gene-specific promoters, changes in ERα Ser118 phosphorylation were assessed for effects on receptor and coregulator recruitment and transcription of ERα-regulated genes. Chromatin immunoprecipitation assays to measure promoter association found a 17β-estradiol (E2)-dependent recruitment of ERα at 150 min to ERα-regulated promoters, whereas ERα phosphorylated at Ser118 was dissociated from promoters after E2 treatment. Mutation of Ser118 to alanine (S118A) altered unliganded and ligand-induced association of ERα and p160 coregulators with ERα target promoters when compared with wild-type (WT)-ERα transfection. S118A and WT-ERα exhibited a similar level of recruitment to the estrogen response element-driven pS2 promoter and induced pS2 mRNA after E2 treatment. Although WT-ERα was recruited to c-myc and cyclin D1 promoters after E2 treatment and induced mRNA expression, S118A exhibited reduced interaction with c-myc and cyclin D1 promoters, and E2 did not induce c-myc and cyclin D1 mRNA. In addition, S118A resulted in increased recruitment of steroid receptor coactivator-1, glucocorticoid receptor interacting protein-1, and activated in breast cancer-1 to pS2, c-myc, and cyclin D1 irrespective of the presence of E2. Together, these data indicate that site specific phosphorylation of ERα directs gene-specific recruitment of ERα and transcriptional coregulators to ERα target gene promoters.

scholarly journals MICoA, a Novel Metastasis-associated Protein 1 (MTA1) Interacting Protein Coactivator, Regulates Estrogen Receptor-α Transactivation Functions

2003 ◽  
Vol 278 (21) ◽  
pp. 19209-19219 ◽  
Author(s):  
Sandip K. Mishra ◽  
Abhijit Mazumdar ◽  
Ratna K. Vadlamudi ◽  
Feng Li ◽  
Rui-An Wang ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Interacting Protein

scholarly journals ARA67/PAT1 Functions as a Repressor To Suppress Androgen Receptor Transactivation

2004 ◽  
Vol 24 (3) ◽  
pp. 1044-1057 ◽  
Author(s):  
Yanqing Zhang ◽  
Yue Yang ◽  
Shuyuan Yeh ◽  
Chawnshang Chang
Keyword(s):  
Prostate Cancer ◽  
Estrogen Receptor ◽  
Androgen Receptor ◽  
Interacting Protein ◽  
N Terminus ◽  
Nuclear Shuttling ◽  
Multiple Domains ◽  
Identification And Characterization ◽  
Receptor Transactivation

ABSTRACT The androgen receptor (AR) may recruit multiple coregulators for proper or optimal transactivation. Here we report the identification and characterization of ARA67/PAT1 as an AR coregulator from a prostate cDNA library. ARA67/PAT1 was screened out as an AR N terminus interacting protein. Interaction mapping shows that the cooperation of multiple domains within ARA67/PAT1 may be required for the maximal interaction with AR. ARA67/PAT1 functions as a repressor with better suppressive effects on AR compared to glucocorticoid receptor and estrogen receptor. Further mechanism dissection reveals that the interrupted AR cytoplasmic-nuclear shuttling may play a major role in ARA67/PAT1 mediated suppression on AR. Together, these results suggest that ARA67/PAT1 may function as a novel repressor that can modulate AR function in prostate cancer.

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