scholarly journals Stimulation of peroxisome proliferator-activated receptor γ inhibits estrogen receptor α transcriptional activity in endometrial carcinoma cells

2015 ◽  
Vol 33 (3) ◽  
pp. 1227-1234 ◽  
Author(s):  
GUIYU ZHANG ◽  
XINXIN HOU ◽  
SHUHONG GAO
Keyword(s):  
Estrogen Receptor ◽  
Endometrial Carcinoma ◽  
Transcriptional Activity ◽  
Estrogen Receptor Α ◽  
Carcinoma Cells ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Stimulation Of

scholarly journals Scaffold attachment factor B1 directly interacts with nuclear receptors in living cells and represses transcriptional activity

2005 ◽  
Vol 35 (3) ◽  
pp. 503-517 ◽  
Author(s):  
M-B Debril ◽  
L Dubuquoy ◽  
J-N Feige ◽  
W Wahli ◽  
B Desvergne ◽  
...  
Keyword(s):  
Nuclear Receptors ◽  
Transcriptional Activity ◽  
Resonance Energy ◽  
Human Adipose Tissue ◽  
Estrogen Receptor Α ◽  
Living Cells ◽  
Peroxisome Proliferator ◽  
Peroxisome Proliferator Activated Receptor ◽  
Attachment Factor

Transcriptional activity relies on coregulators that modify the chromatin structure and serve as bridging factors between transcription factors and the basal transcription machinery. Using the DE domain of human peroxisome proliferator-activated receptor gamma (PPARγ) as bait in a yeast two-hybrid screen of a human adipose tissue library, we isolated the scaffold attachment factor B1 (SAFB1/HET/HAP), which was previously shown to be a corepressor of estrogen receptor α. We show here that SAFB1 has a very broad tissue expression profile in human and is also expressed all along mouse embryogenesis. SAFB1 interacts in pull-down assays not only with PPARγ but also with all nuclear receptors tested so far, albeit with different affinities. The association of SAFB1 and PPARγ in vivo is further demonstrated by fluorescence resonance energy transfer (FRET) experiments in living cells. We finally show that SAFB1 is a rather general corepressor for nuclear receptors. Its change in expression during the early phases of adipocyte and enterocyte differentiation suggests that SAFB1 potentially influences cell proliferation and differentiation decisions.

scholarly journals The Role of Nuclear Receptors in Prostate Cancer

Cells ◽  
2019 ◽  
Vol 8 (6) ◽  
pp. 602 ◽  
Author(s):  
Masaki Shiota ◽  
Naohiro Fujimoto ◽  
Eiji Kashiwagi ◽  
Masatoshi Eto
Keyword(s):  
Prostate Cancer ◽  
Estrogen Receptor ◽  
Androgen Receptor ◽  
Estrogen Receptor Α ◽  
Peroxisome Proliferator ◽  
Biological Processes ◽  
Peroxisome Proliferator Activated Receptor ◽  
Functional Roles ◽  
Cancer Pathogenesis

The nuclear receptor (NR) superfamily consists of 48 members that are divided into seven subfamilies. NRs are transcription factors that play an important role in a number of biological processes. The NR superfamily includes androgen receptor, which is a key player in prostate cancer pathogenesis, suggesting the functional roles of other NRs in prostate cancer. The findings on the roles of NRs in prostate cancer thus far have shown that several NRs such as vitamin D receptor, estrogen receptor β, and mineralocorticoid receptor play antioncogenic roles, while other NRs such as peroxisome proliferator-activated receptor γ and estrogen receptor α as well as androgen receptor play oncogenic roles. However, the roles of other NRs in prostate cancer remain controversial or uninvestigated. Further research on the role of NRs in prostate cancer is required and may lead to the development of novel preventions and therapeutics for prostate cancer.

scholarly journals Differential Regulation of Estrogen-Inducible Proteolysis and Transcription by the Estrogen Receptor α N Terminus

2005 ◽  
Vol 25 (13) ◽  
pp. 5417-5428 ◽  
Author(s):  
Christopher C. Valley ◽  
Raphaël Métivier ◽  
Natalia M. Solodin ◽  
Amy M. Fowler ◽  
Mara T. Mashek ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Transcriptional Activity ◽  
Target Genes ◽  
Estrogen Receptor Α ◽  
Transactivation Domain ◽  
Related Factors ◽  
Additional Element ◽  
Transactivation Domains ◽  
Ubiquitin Proteasome ◽  
Transcriptional Complex

ABSTRACT The ubiquitin-proteasome pathway has emerged as an important regulatory mechanism governing the activity of several transcription factors. While estrogen receptor α (ERα) is also subjected to rapid ubiquitin-proteasome degradation, the relationship between proteolysis and transcriptional regulation is incompletely understood. Based on studies primarily focusing on the C-terminal ligand-binding and AF-2 transactivation domains, an assembly of an active transcriptional complex has been proposed to signal ERα proteolysis that is in turn necessary for its transcriptional activity. Here, we investigated the role of other regions of ERα and identified S118 within the N-terminal AF-1 transactivation domain as an additional element for regulating estrogen-induced ubiquitination and degradation of ERα. Significantly, different S118 mutants revealed that degradation and transcriptional activity of ERα are mechanistically separable functions of ERα. We find that proteolysis of ERα correlates with the ability of ERα mutants to recruit specific ubiquitin ligases regardless of the recruitment of other transcription-related factors to endogenous model target genes. Thus, our findings indicate that the AF-1 domain performs a previously unrecognized and important role in controlling ligand-induced receptor degradation which permits the uncoupling of estrogen-regulated ERα proteolysis and transcription.

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