Show simple item record

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.
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
html.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.


This item appears in the following Collection(s)

Show simple item record