ArticleMolecular and cellular biology1998
ETS-mediated cooperation between basic helix-loop-helix motifs of the immunoglobulin mu heavy-chain gene enhancer.
Article in Molecular and cellular biology, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed, 28 citations in OpenAlex.
- Recombination may occur in the absence of transcription in the immunoglobulin heavy chain recombination centre.Nucleic acids research · 2020Article
- Transcription factors with conserved binding sites near ATOH1 on the POU4F3 gene enhance the induction of cochlear hair cells.Molecular neurobiology · 2015Article
- Targeting of somatic hypermutation by immunoglobulin enhancer and enhancer-like sequences.PLoS biology · 2014Article
- Identification of interacting transcription factors regulating tissue gene expression in human.BMC genomics · 2010Article
- Differential regulation of epithelial and mesenchymal markers by deltaEF1 proteins in epithelial mesenchymal transition induced by TGF-beta.Molecular biology of the cell · 2007Article
- Combinatorial gene control involving E2F and E Box family members.The EMBO journal · 2004Article
- Review
- Transcriptional activation by ETS and leucine zipper-containing basic helix-loop-helix proteins.Molecular and cellular biology · 1999Article
- Id helix-loop-helix proteins inhibit nucleoprotein complex formation by the TCF ETS-domain transcription factors.The EMBO journal · 1999Article
- Exploring functional redundancy in the immunoglobulin mu heavy-chain gene enhancer.Molecular and cellular biology · 1998Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
The muE motifs of the immunoglobulin mu heavy-chain gene enhancer bind ubiquitously expressed proteins of the basic helix-loop-helix (bHLH) family. These elements work together with other, more tissue-restricted elements to produce B-cell-specific enhancer activity by presently undefined combinatorial mechanisms. We found that muE2 contributed to transcription activation in B cells only when the muE3 site was intact, providing the first evidence for functional interactions between bHLH proteins. In vitro assays showed that bHLH zipper proteins binding to muE3 enhanced Ets-1 binding to muA. One of the consequences of this protein-protein interaction was to facilitate binding of a second bHLH protein, E47, to the muE2 site, thereby generating a three-protein-DNA complex. Furthermore, transcriptional synergy between bHLH and bHLH zipper factors also required an intermediate ETS protein, which may bridge the transcription activation domains of the bHLH factors. Our observations define an unusual form of cooperation between bHLH and ETS proteins and suggest mechanisms by which tissue-restricted and ubiquitous factors combine to generate tissue-specific enhancer activity.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.