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
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
PubMed ID: 7744009
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