Id helix-loop-helix proteins antagonize pax transcription factor activity by inhibiting DNA binding.

2.50
Hdl Handle:
http://hdl.handle.net/10541/85766
Title:
Id helix-loop-helix proteins antagonize pax transcription factor activity by inhibiting DNA binding.
Authors:
Roberts, E Claire; Deed, Richard W; Inoue, Toshiaki; 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. The major mechanism by which Id proteins are thought to inhibit differentiation is through interaction with other HLH proteins and inhibition of their DNA-binding activity. However, Id proteins have also been shown to interact with other proteins involved in regulating cellular proliferation and differentiation, suggesting a more widespread regulatory function. In this study we demonstrate functional interactions between Id proteins and members of the Pax-2/-5/-8 subfamily of paired-domain transcription factors. Members of the Pax transcription factor family have key functions in regulating several developmental processes exemplified by B lymphopoiesis, in which Pax-5 plays an essential role. Id proteins bind to Pax proteins in vitro and in vivo. Binding occurs through the paired DNA-binding domain of the Pax proteins and results in the disruption of DNA-bound complexes containing Pax-2, Pax-5, and Pax-8. In vivo, Id proteins modulate the transcriptional activity mediated by Pax-5 complexes on the B-cell-specific mb-1 promoter. Our results therefore demonstrate a novel facet of Id function in regulating cellular differentiation by functionally antagonizing the action of members of the Pax transcription factor family.
Affiliation:
Department of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, United Kingdom.
Citation:
Id helix-loop-helix proteins antagonize pax transcription factor activity by inhibiting DNA binding. 2001, 21 (2):524-33 Mol. Cell. Biol.
Journal:
Molecular and Cellular Biology
Issue Date:
Jan-2001
URI:
http://hdl.handle.net/10541/85766
DOI:
10.1128/MCB.21.2.524-533.2001
PubMed ID:
11134340
Type:
Article
Language:
en
ISSN:
0270-7306
Appears in Collections:
All Paterson Institute for Cancer Research

Full metadata record

DC FieldValue Language
dc.contributor.authorRoberts, E Claireen
dc.contributor.authorDeed, Richard Wen
dc.contributor.authorInoue, Toshiakien
dc.contributor.authorNorton, John Den
dc.contributor.authorSharrocks, Andrew Den
dc.date.accessioned2009-11-10T10:42:24Z-
dc.date.available2009-11-10T10:42:24Z-
dc.date.issued2001-01-
dc.identifier.citationId helix-loop-helix proteins antagonize pax transcription factor activity by inhibiting DNA binding. 2001, 21 (2):524-33 Mol. Cell. Biol.en
dc.identifier.issn0270-7306-
dc.identifier.pmid11134340-
dc.identifier.doi10.1128/MCB.21.2.524-533.2001-
dc.identifier.urihttp://hdl.handle.net/10541/85766-
dc.description.abstractThe Id subfamily of helix-loop-helix (HLH) proteins plays a fundamental role in the regulation of cellular proliferation and differentiation. The major mechanism by which Id proteins are thought to inhibit differentiation is through interaction with other HLH proteins and inhibition of their DNA-binding activity. However, Id proteins have also been shown to interact with other proteins involved in regulating cellular proliferation and differentiation, suggesting a more widespread regulatory function. In this study we demonstrate functional interactions between Id proteins and members of the Pax-2/-5/-8 subfamily of paired-domain transcription factors. Members of the Pax transcription factor family have key functions in regulating several developmental processes exemplified by B lymphopoiesis, in which Pax-5 plays an essential role. Id proteins bind to Pax proteins in vitro and in vivo. Binding occurs through the paired DNA-binding domain of the Pax proteins and results in the disruption of DNA-bound complexes containing Pax-2, Pax-5, and Pax-8. In vivo, Id proteins modulate the transcriptional activity mediated by Pax-5 complexes on the B-cell-specific mb-1 promoter. Our results therefore demonstrate a novel facet of Id function in regulating cellular differentiation by functionally antagonizing the action of members of the Pax transcription factor family.en
dc.language.isoenen
dc.subjectCancer Proteinsen
dc.subject.mesh3T3 Cells-
dc.subject.meshAnimals-
dc.subject.meshAntigens, CD-
dc.subject.meshAntigens, CD79-
dc.subject.meshB-Cell-Specific Activator Protein-
dc.subject.meshBase Sequence-
dc.subject.meshCOS Cells-
dc.subject.meshDNA-
dc.subject.meshDNA-Binding Proteins-
dc.subject.meshGene Expression Regulation-
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.meshPAX2 Transcription Factor-
dc.subject.meshPaired Box Transcription Factors-
dc.subject.meshPrecipitin Tests-
dc.subject.meshPromoter Regions, Genetic-
dc.subject.meshProtein Binding-
dc.subject.meshProto-Oncogene Proteins-
dc.subject.meshReceptors, Antigen, B-Cell-
dc.subject.meshRepressor Proteins-
dc.subject.meshTrans-Activators-
dc.subject.meshTranscription Factors-
dc.subject.meshets-Domain Protein Elk-1-
dc.titleId helix-loop-helix proteins antagonize pax transcription factor activity by inhibiting DNA binding.en
dc.typeArticleen
dc.contributor.departmentDepartment of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, United Kingdom.en
dc.identifier.journalMolecular and Cellular Biologyen

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