The ETS Family Member TEL Binds to Nuclear Receptors RAR and RXR and Represses Gene Activation

被引：5

作者：

Meester-Smoor, Magda A. ^{[1
]}

Janssen, Marjolein J. F. W. ^{[1
]}

ter Haar, W. Martijn ^{[1
]}

van Wely, Karel H. M. ^{[1
]}

Aarnoudse, Albert-Jan L. H. J. ^{[1
]}

van Oord, Gertine ^{[1
]}

van Tilburg, Gabrielle B. A. ^{[1
]}

Zwarthoff, Ellen C. ^{[1
]}

机构：

[1] Erasmus MC, Josephine Nefkens Inst, Dept Pathol, Rotterdam, Netherlands

来源：

PLOS ONE | 2011年 / 6卷 / 09期

关键词：

LONG TERMINAL REPEAT; DNA-BINDING; TRANSCRIPTIONAL REPRESSOR; MEDIATED TRANSCRIPTION; MYELOID-LEUKEMIA; FUSION PROTEIN; N-COR; ONCOPROTEIN; TRANSLOCATION; COACTIVATORS;

D O I：

10.1371/journal.pone.0023620

中图分类号：

O [数理科学和化学]; P [天文学、地球科学]; Q [生物科学]; N [自然科学总论];

学科分类号：

07 ; 0710 ; 09 ;

摘要：

Retinoic acid receptor (RAR) signaling is important for regulating transcriptional activity of genes involved in growth, differentiation, metabolism and reproduction. Defects in RAR signaling have been implicated in cancer. TEL, a member of the ETS family of transcription factors, is a DNA-binding transcriptional repressor. Here, we identify TEL as a transcriptional repressor of RAR signaling by its direct binding to both RAR and its dimerisation partner, the retinoid x receptor (RXR) in a ligand-independent fashion. TEL is found in two isoforms, created by the use of an alternative startcodon at amino acid 43. Although both isoforms bind to RAR and RXR in vitro and in vivo, the shorter form of TEL represses RAR signaling much more efficiently. Binding studies revealed that TEL binds closely to the DNA binding domain of RAR and that both Helix Loop Helix (HLH) and DNA binding domains of TEL are mandatory for interaction. We have shown that repression by TEL does not involve recruitment of histone deacetylases and suggest that polycomb group proteins participate in the process.

引用

页数：7