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

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.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Calcium-Binding Proteins, DNA, Complementary, Humans, In Vitro Techniques, Mice, Molecular Sequence Data, Oncogene Proteins, Viral, Papillomaviridae, Receptors, Calcitriol, Recombinant Fusion Proteins, Saccharomyces cerevisiae, Sequence Homology, Amino Acid
Biochem. Biophys. Res. Commun.
Date: Apr. 28, 1997
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