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 ERα α α α is maintained silent in gene regulation upon the target gene promoters, we biochemically searched interactants for hERα α α α, 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 hERα α α α, and thereby deters hERα α α α from recruiting transcriptional coregulators, presumably as a component of chaperone complexes.
Retraction: The above article in Genes to Cells (doi: ), published online on 13 October 2005 in Wiley Online Library (http://onlinelibrary.wiley.com/), has been retracted by agreement between the authors, the journal Editor in Chief, Mitsuhiro Yanagida, and Wiley Publishing Asia Pty Ltd. The retraction has been agreed to due to lack of the gel images for the lanes 1, 2 and 3 of ‘αTRAP220’ and for the lanes 1, 2 and 4 of ‘αHsc70’ in Figure 4(A).
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