The N-terminal part of TIF1, a putative mediator of the ligand-dependent activation function (AF-2) of nuclear receptors, is fused to B-raf in the oncogenic protein T18.

Nuclear receptors (NRs) bound to response elements mediate the effects of cognate ligands on gene expression. Their ligand-dependent activation function, AF-2, presumably acts on the basal transcription machinery through intermediary proteins/mediators. We have isolated a mouse nuclear protein, TIF1, which enhances RXR and RAR AF-2 in yeast and interacts in ...
a ligand-dependent manner with several NRs in yeast and mammalian cells, as well as in vitro. Remarkably, these interactions require the amino acids constituting the AF-2 activating domain conserved in all active NRs. Moreover, the oestrogen receptor (ER) AF-2 antagonist hydroxytamoxifen cannot promote ER-TIF1 interaction. We propose that TIF1, which contains several conserved domains found in transcriptional regulatory proteins, is a mediator of ligand-dependent AF-2. Interestingly, the TIF1 N-terminal moiety is fused to B-raf in the mouse oncoprotein T18.
Mesh Terms:
Amino Acid Sequence, Animals, Base Sequence, Cloning, Molecular, Conserved Sequence, DNA, Complementary, DNA, Fungal, Evolution, Ligands, Mice, Molecular Sequence Data, Nuclear Proteins, Protein-Serine-Threonine Kinases, Proto-Oncogene Proteins, Proto-Oncogene Proteins c-raf, Receptors, Cytoplasmic and Nuclear, Receptors, Retinoic Acid, Retinoid X Receptors, Saccharomyces cerevisiae, Sequence Homology, Amino Acid, Transcription Factors
EMBO J.
Date: May. 01, 1995
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