| Autor: |
Creekmore AL; Department of Cell and Developmental Biology, University of Illinois, Urbana, IL 61801, United States., Walt KA, Schultz-Norton JR, Ziegler YS, McLeod IX, Yates JR, Nardulli AM |
| Jazyk: |
angličtina |
| Zdroj: |
Molecular and cellular endocrinology [Mol Cell Endocrinol] 2008 Sep 10; Vol. 291 (1-2), pp. 79-86. Date of Electronic Publication: 2008 Jun 05. |
| DOI: |
10.1016/j.mce.2008.05.016 |
| Abstrakt: |
The differential recruitment of coregulatory proteins to the DNA-bound estrogen receptor alpha (ERalpha) plays a critical role in mediating estrogen-responsive gene expression. We previously isolated and identified retinoblastoma-associated proteins 46 (RbAp46) and 48 (RbAp48), which are associated with chromatin remodeling, histone deacetylation, and transcription repression, as proteins associated with the DNA-bound ERalpha. We now demonstrate that RbAp46 and RbAp48 interact with ERalphain vitro and in vivo, associate with ERalpha at endogenous, estrogen-responsive genes, and alter expression of endogenous, ERalpha-activated and -repressed genes in MCF-7 breast cancer cells. Our findings reveal that RbAp48 limits expression of estrogen-responsive genes and that RbAp46 modulates estrogen responsiveness in a gene-specific manner. The ability of RbAp46 and RbAp48 to interact with ERalpha and influence its activity reveals yet another role for these multifunctional proteins in regulating gene expression. |
| Databáze: |
MEDLINE |
| Externí odkaz: |
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