Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors.

2.50
Hdl Handle:
http://hdl.handle.net/10541/90791
Title:
Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors.
Authors:
Yates, Paula R; Atherton, Graham T; Deed, Richard W; Norton, John D; Sharrocks, Andrew D
Abstract:
The Id subfamily of helix-loop-helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA-binding activity. Members of the ternary complex factor (TCF) subfamily of ETS-domain proteins have key functions in regulating immediate-early gene expression in response to mitogenic stimulation. TCFs form DNA-bound complexes with the serum response factor (SRF) and are direct targets of MAP kinase (MAPK) signal transduction cascades. In this study we demonstrate functional interactions between Id proteins and TCFs. Ids bind to the ETS DNA-binding domain and disrupt the formation of DNA-bound complexes between TCFs and SRF on the c-fos serum response element (SRE). Inhibition occurs by disrupting protein-DNA interactions with the TCF component of this complex. In vivo, the Id proteins cause down-regulation of the transcriptional activity mediated by the TCFs and thereby block MAPK signalling to SREs. Therefore, our results demonstrate a novel facet of Id function in the coordination of mitogenic signalling and cell cycle entry.
Affiliation:
Department of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne, NE2 4HH.
Citation:
Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors. 1999, 18 (4):968-76 EMBO J.
Journal:
EMBO Journal
Issue Date:
15-Feb-1999
URI:
http://hdl.handle.net/10541/90791
DOI:
10.1093/emboj/18.4.968
PubMed ID:
10022839
Type:
Article
Language:
en
ISSN:
0261-4189
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorYates, Paula Ren
dc.contributor.authorAtherton, Graham Ten
dc.contributor.authorDeed, Richard Wen
dc.contributor.authorNorton, John Den
dc.contributor.authorSharrocks, Andrew Den
dc.date.accessioned2010-01-28T11:23:50Z-
dc.date.available2010-01-28T11:23:50Z-
dc.date.issued1999-02-15-
dc.identifier.citationId helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors. 1999, 18 (4):968-76 EMBO J.en
dc.identifier.issn0261-4189-
dc.identifier.pmid10022839-
dc.identifier.doi10.1093/emboj/18.4.968-
dc.identifier.urihttp://hdl.handle.net/10541/90791-
dc.description.abstractThe Id subfamily of helix-loop-helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. Id proteins are thought to inhibit differentiation mainly through interaction with other HLH proteins and by blocking their DNA-binding activity. Members of the ternary complex factor (TCF) subfamily of ETS-domain proteins have key functions in regulating immediate-early gene expression in response to mitogenic stimulation. TCFs form DNA-bound complexes with the serum response factor (SRF) and are direct targets of MAP kinase (MAPK) signal transduction cascades. In this study we demonstrate functional interactions between Id proteins and TCFs. Ids bind to the ETS DNA-binding domain and disrupt the formation of DNA-bound complexes between TCFs and SRF on the c-fos serum response element (SRE). Inhibition occurs by disrupting protein-DNA interactions with the TCF component of this complex. In vivo, the Id proteins cause down-regulation of the transcriptional activity mediated by the TCFs and thereby block MAPK signalling to SREs. Therefore, our results demonstrate a novel facet of Id function in the coordination of mitogenic signalling and cell cycle entry.en
dc.language.isoenen
dc.subjectCancer Proteinsen
dc.subject.mesh3T3 Cells-
dc.subject.meshAnimals-
dc.subject.meshDNA-Binding Proteins-
dc.subject.meshGene Expression Regulation-
dc.subject.meshGenes, fos-
dc.subject.meshHelix-Loop-Helix Motifs-
dc.subject.meshInhibitor of Differentiation Protein 1-
dc.subject.meshInhibitor of Differentiation Protein 2-
dc.subject.meshInhibitor of Differentiation Proteins-
dc.subject.meshMice-
dc.subject.meshNeoplasm Proteins-
dc.subject.meshNuclear Proteins-
dc.subject.meshOligodeoxyribonucleotides-
dc.subject.meshPromoter Regions, Genetic-
dc.subject.meshProto-Oncogene Proteins-
dc.subject.meshRNA, Messenger-
dc.subject.meshRepressor Proteins-
dc.subject.meshSerum Response Factor-
dc.subject.meshTranscription Factors-
dc.subject.meshets-Domain Protein Elk-1-
dc.subject.meshets-Domain Protein Elk-4-
dc.titleId helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors.en
dc.typeArticleen
dc.contributor.departmentDepartment of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne, NE2 4HH.en
dc.identifier.journalEMBO Journalen

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