| Erg proteins, transcription factors of the Ets family, form homo, heterodimers and ternary complexes via two distinct domains. | |
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MedLine Citation:
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PMID: 9681824 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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The ets genes family encodes a group of proteins which function as transcription factors under physiological conditions. We report here that the Erg proteins, members of the Ets family, form homo and heterodimeric complexes in vitro. We demonstrate that the Ergp55 protein isoform forms dimers with itself and with the two other isoforms, Ergp49 and Ergp38. Using a set of Erg protein deletion mutants, we define two distinct domains independently involved in dimerization. The first one is located in the amino-terminal part of the protein containing the pointed domain (PNT), conserved in a subset of Ets proteins. The second one resides within the ETS domain, the DNA-binding domain. We also show that the Erg protein central region behaves as an inhibitory domain of dimerization and its removal enhances the Ergp55 transactivation properties. Furthermore, Ergp55 forms heterodimers with some other Ets proteins. Among the latter, we show that Fli-1, Ets-2, Er81 and Pu-1 physically interact with Erg. Finally, we show that the formation of the previously described ternary complex Ergp55/Fos/jun is mediated by ETS domain and Jun protein, while the ternary complex Ergp49/Fos/Jun is mediated by Fos protein. |
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Authors:
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S Carrère; A Verger; A Flourens; D Stehelin; M Duterque-Coquillaud |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't |
Journal Detail:
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Title: Oncogene Volume: 16 ISSN: 0950-9232 ISO Abbreviation: Oncogene Publication Date: 1998 Jun |
Date Detail:
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Created Date: 1998-08-04 Completed Date: 1998-08-04 Revised Date: 2008-11-21 |
Medline Journal Info:
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Nlm Unique ID: 8711562 Medline TA: Oncogene Country: ENGLAND |
Other Details:
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Languages: eng Pagination: 3261-8 Citation Subset: IM |
Affiliation:
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CNRS UMR 319, Institut de Biologie de Lille, France. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Binding Sites Biopolymers / chemistry DNA-Binding Proteins / metabolism Dimerization Gene Deletion Humans Mutation / genetics, physiology Oncogene Proteins / chemistry*, genetics, metabolism Protein Binding Protein Conformation Protein Structure, Tertiary Retroviridae Proteins, Oncogenic / chemistry*, metabolism Trans-Activators* Transcription Factor AP-1 / metabolism Transcription Factors / chemistry*, metabolism Transcriptional Activation / drug effects, genetics, physiology Tumor Cells, Cultured |
| Chemical | |
Reg. No./Substance:
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0/Biopolymers; 0/DNA-Binding Proteins; 0/ERG protein, human; 0/Oncogene Proteins; 0/Retroviridae Proteins, Oncogenic; 0/Trans-Activators; 0/Transcription Factor AP-1; 0/Transcription Factors; 0/oncogene proteins v-ets |
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine
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