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

被引：556

作者：

LEDOUARIN, B ^{[1
]}

ZECHEL, C ^{[1
]}

GARNIER, JM ^{[1
]}

LUTZ, Y ^{[1
]}

TORA, L ^{[1
]}

PIERRAT, B ^{[1
]}

HEERY, D ^{[1
]}

GRONEMEYER, H ^{[1
]}

CHAMBON, P ^{[1
]}

LOSSON, R ^{[1
]}

机构：

[1] ULP, COLL FRANCE,CNRS,INSERM, INST GENET & BIOL MOLEC & CELLULAIRE, F-67404 ILLKIRCH GRAFFENSTADEN, FRANCE

来源：

EMBO JOURNAL | 1995年 / 14卷 / 09期

关键词：

BROMODOMAIN; NUCLEAR RECEPTORS; ONCOPROTEIN; RING FINGER; TRANSCRIPTIONAL INTERMEDIARY FACTOR;

D O I：

10.1002/j.1460-2075.1995.tb07194.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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.

引用

页码：2020 / 2033

页数：14

共 81 条

[1] PRODUCTION AND CHARACTERIZATION OF MONOCLONAL-ANTIBODIES RECOGNIZING DEFINED REGIONS OF THE HUMAN ESTROGEN-RECEPTOR [J].