Document Detail

Repressive domain of unliganded human estrogen receptor alpha associates with Hsc70.
MedLine Citation:
PMID:  16324147     Owner:  NLM     Status:  MEDLINE    
Estrogen receptor (ER) is a hormone-inducible transcription factor as a member of the nuclear receptor gene superfamily. Unliganded ER is transcriptionally silent and capable of DNA binding; however, it is unable to suppress the basal activity of the target gene promoters, unlike non-steroid hormone receptors that associate with corepressors in the absence of their cognate ligands. To study the molecular basis of how unliganded human ERalpha is maintained silent in gene regulation upon the target gene promoters, we biochemically searched interactants for hERalpha, and identified heat shock protein 70 (Hsc70). Hsc70 appeared to associate with the N-terminal hormone binding E domain, that also turned out a transcriptionally repressive domain. Competitive association of Hsc70 with a best known coactivator p300 was observed. Thus, these findings suggest that Hsc70 associates with unliganded hERalpha, and thereby deters hERalpha from recruiting transcriptional coregulators, presumably as a component of chaperone complexes.
Satoko Ogawa; Hajime Oishi; Yoshihiro Mezaki; Madoka Kouzu-Fujita; Reiko Matsuyama; Madoka Nakagomi; Eri Mori; Emi Murayama; Hiromichi Nagasawa; Hirochika Kitagawa; Junn Yanagisawa; Tetsu Yano; Shigeaki Kato
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Retracted Publication    
Journal Detail:
Title:  Genes to cells : devoted to molecular & cellular mechanisms     Volume:  10     ISSN:  1356-9597     ISO Abbreviation:  Genes Cells     Publication Date:  2005 Dec 
Date Detail:
Created Date:  2005-12-05     Completed Date:  2006-04-24     Revised Date:  2014-03-24    
Medline Journal Info:
Nlm Unique ID:  9607379     Medline TA:  Genes Cells     Country:  England    
Other Details:
Languages:  eng     Pagination:  1095-102     Citation Subset:  IM    
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MeSH Terms
Cells, Cultured
Estrogen Receptor alpha / chemistry,  genetics,  metabolism*
Fluorescent Antibody Technique
Gene Expression Regulation
HSP70 Heat-Shock Proteins / genetics,  metabolism*
HeLa Cells
Molecular Chaperones / genetics,  metabolism
Nuclear Proteins / genetics,  metabolism
Protein Binding / genetics
Protein Interaction Mapping
Protein Structure, Tertiary / genetics,  physiology
Recombinant Fusion Proteins / genetics,  metabolism
Repressor Proteins / genetics,  metabolism*
Transcription, Genetic
Transcriptional Activation / genetics
Reg. No./Substance:
0/Estrogen Receptor alpha; 0/HSP70 Heat-Shock Proteins; 0/Ligands; 0/Molecular Chaperones; 0/Nuclear Proteins; 0/Recombinant Fusion Proteins; 0/Repressor Proteins
Retraction In:
Genes Cells. 2013 Dec;18(12):1145   [PMID:  24654281 ]

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