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| 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 |
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| Author(s): LEDOUARIN B, ZECHEL C, GARNIER JM, LUTZ Y, TORA L, PIERRAT B, HEERY D, GRONEMEYER H, CHAMBON P, LOSSON R |
| Source: EMBO JOURNAL Volume: 14 Issue: 9 Pages: 2020-2033 Published: MAY 1 1995 |
| Times Cited: 479 References: 81 |
| Abstract: 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. |
| Document Type: Article |
| Language: English |
Addresses:
1. ULP, COLL FRANCE, CNRS, INSERM, INST GENET & BIOL MOLEC & CELLULAIRE, F-67404 ILLKIRCH GRAFFENSTADEN, FRANCE |
| Publisher: OXFORD UNIV PRESS UNITED KINGDOM, WALTON ST JOURNALS DEPT, OXFORD, ENGLAND OX2 6DP |
| Subject Category: Biochemistry & Molecular Biology; Cell Biology |
| IDS Number: QX744 |
| ISSN: 0261-4189 |
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