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ERC-55, a binding protein for the papilloma virus E6 oncoprotein, specifically interacts with vitamin D receptor among nuclear receptors.

Abstract：

:VDR regulates gene expression in a ligand-dependent way by binding to cognate enhancer elements of target gene promoters. The ligand-dependent activation function, AF-2, of VDR is thought to require transcriptional co-activators/co-repressors together with basal transcriptional machinery. Using a yeast two hybrid system with VDR, we have isolated a mouse Ca(2+)-binding protein (designated as VAF1) specifically interacting in vivo and in vitro with VDR among nuclear receptors like RAR, RXR, ER and GR. VAF1 is a mouse homologue to human ERC-55, which has recently been shown to interact with human papillomavirus oncogenic protein, E6[1]. Unlike those of many previously identified co-activators, the VDR-VAF1 interaction was ligand-independent. Thus, VAF1 seems a putative VDR-specific cofactor modulating its function.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Imai T,Matsuda K,Shimojima T,Hashimoto T,Masuhiro Y,Kitamoto T,Sugita A,Suzuki K,Matsumoto H,Masushige S,Nogi Y,Muramatsu M,Handa H,Kato S

doi

10.1006/bbrc.1997.6531

subject

Has Abstract

pub_date

1997-04-28 00:00:00

pages

765-9

issue

3

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(97)96531-1

journal_volume

233

pub_type

杂志文章

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