Id helix-loop-helix proteins antagonize pax transcription factor activity by inhibiting DNA binding.
Affiliation
Department of Biochemistry and Genetics, The Medical School, University of Newcastle upon Tyne, Newcastle upon Tyne NE2 4HH, United Kingdom.Issue Date
2001-01
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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.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 BiologyDOI
10.1128/MCB.21.2.524-533.2001PubMed ID
11134340Type
ArticleLanguage
enISSN
0270-7306ae974a485f413a2113503eed53cd6c53
10.1128/MCB.21.2.524-533.2001
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