scholarly journals Estrogen-Enhanced Peptidylarginine Deiminase Type IV Gene (PADI4) Expression in MCF-7 Cells Is Mediated by Estrogen Receptor-α-Promoted Transfactors Activator Protein-1, Nuclear Factor-Y, and Sp1

2007 ◽  
Vol 21 (7) ◽  
pp. 1617-1629 ◽  
Author(s):  
Sijun Dong ◽  
Zilian Zhang ◽  
Hidenari Takahara
Keyword(s):  
Estrogen Receptor ◽  
Estrogen Receptor Α ◽  
Nuclear Factor ◽  
Activator Protein 1 ◽  
Peptidylarginine Deiminase ◽  
Nuclear Factor Y ◽  
Activator Protein ◽  
Type Iv ◽  
Mcf 7

scholarly journals Estrogen receptor-α mediates human multidrug resistance associated protein 3 induction by 17α-ethynylestradiol. Role of activator protein-1

2013 ◽  
Vol 86 (3) ◽  
pp. 401-409 ◽  
Author(s):  
María Laura Ruiz ◽  
Juan Pablo Rigalli ◽  
Agostina Arias ◽  
Silvina Stella Maris Villanueva ◽  
Claudia Banchio ◽  
...  
Keyword(s):  
Estrogen Receptor ◽  
Multidrug Resistance ◽  
Estrogen Receptor Α ◽  
Activator Protein 1 ◽  
Activator Protein

scholarly journals PARP7 and Mono-ADP-Ribosylation Negatively Regulate Estrogen Receptor α Signaling in Human Breast Cancer Cells

Cells ◽  
2021 ◽  
Vol 10 (3) ◽  
pp. 623
Author(s):  
Marit Rasmussen ◽  
Susanna Tan ◽  
Venkata S. Somisetty ◽  
David Hutin ◽  
Ninni Elise Olafsen ◽  
...  
Keyword(s):  
Breast Cancer ◽  
Estrogen Receptor ◽  
Protein Modification ◽  
Target Genes ◽  
Estrogen Receptor Α ◽  
Transactivation Domain ◽  
Adp Ribosylation ◽  
Protein Levels ◽  
17Β Estradiol ◽  
Mcf 7

ADP-ribosylation is a post-translational protein modification catalyzed by a family of proteins known as poly-ADP-ribose polymerases. PARP7 (TIPARP; ARTD14) is a mono-ADP-ribosyltransferase involved in several cellular processes, including responses to hypoxia, innate immunity and regulation of nuclear receptors. Since previous studies suggested that PARP7 was regulated by 17β-estradiol, we investigated whether PARP7 regulates estrogen receptor α signaling. We confirmed the 17β-estradiol-dependent increases of PARP7 mRNA and protein levels in MCF-7 cells, and observed recruitment of estrogen receptor α to the promoter of PARP7. Overexpression of PARP7 decreased ligand-dependent estrogen receptor α signaling, while treatment of PARP7 knockout MCF-7 cells with 17β-estradiol resulted in increased expression of and recruitment to estrogen receptor α target genes, in addition to increased proliferation. Co-immunoprecipitation assays revealed that PARP7 mono-ADP-ribosylated estrogen receptor α, and mass spectrometry mapped the modified peptides to the receptor’s ligand-independent transactivation domain. Co-immunoprecipitation with truncated estrogen receptor α variants identified that the hinge region of the receptor is required for PARP7-dependent mono-ADP-ribosylation. These results imply that PARP7-mediated mono-ADP-ribosylation may play an important role in estrogen receptor positive breast cancer.

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