ArticleMolecular and cellular biology1996
Drosophila homologs of the proto-oncogene product PEBP2/CBF beta regulate the DNA-binding properties of Runt.
Article in Molecular and cellular biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
27 citing papers in PubMed, 92 citations in OpenAlex.
- Regulatory diversification of conservedZoological research · 2026Article
- "A Friend Among Strangers" or the Ambiguous Roles of Runx2.Biomolecules · 2024Review
- Article
- The transcription factor Bcl11b promotes both canonical and adaptive NK cell differentiation.Science immunology · 2021Article
- Transcriptional Programming in Arteriosclerotic Disease: A Multifaceted Function of the Runx2 (Runt-Related Transcription Factor 2).Arteriosclerosis, thrombosis, and vascular biology · 2021Review
- Wrong place, wrong time: Runt-related transcription factor 2/SATB2 pathway in bone development and carcinogenesis.Journal of carcinogenesis · 2021Review
- RUNX1-dependent mechanisms in biological control and dysregulation in cancer.Journal of cellular physiology · 2019Review
- RUNX1-ETO: Attacking the Epigenome for Genomic Instable Leukemia.International journal of molecular sciences · 2019Review
- Cbfβ2 controls differentiation of and confers homing capacity to prethymic progenitors.The Journal of experimental medicine · 2018Article
- Characterization of the Runx gene family in a jawless vertebrate, the Japanese lamprey (Lethenteron japonicum).PloS one · 2014Article
- HIV type 1 viral infectivity factor and the RUNX transcription factors interact with core binding factor β on genetically distinct surfaces.AIDS research and human retroviruses · 2012Article
- Hairless is a cofactor for Runt-dependent transcriptional regulation.Molecular biology of the cell · 2011Article
- Alternative splicing removes an Ets interaction domain from Lozenge during Drosophila eye development.Development genes and evolution · 2005Article
- A bacterial one-hybrid system for determining the DNA-binding specificity of transcription factors.Nature biotechnology · 2005Article
- Oncogenic potential of the RUNX gene family: 'overview'.Oncogene · 2004Review
- Cooperation between the GATA and RUNX factors Serpent and Lozenge during Drosophila hematopoiesis.The EMBO journal · 2003Article
- Multimerization via its myosin domain facilitates nuclear localization and inhibition of core binding factor (CBF) activities by the CBFbeta-smooth muscle myosin heavy chain myeloid leukemia oncoprotein.Molecular and cellular biology · 2002Article
- Article
- Common themes in the pathogenesis of acute myeloid leukemia.Oncogene · 2001Review
- Review
Corrections and comments
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Authors and funding
5 authors at 1 institution in 1 country.
Funding
Abstract
The Drosophila runt gene is the founding member of the Runt domain family of transcriptional regulators. Mammalian Runt domain genes encode the alpha subunit of the heterometric DNA-binding factor PEBP2/CBF. The unrelated PEBP2/CBF beta protein interacts with the Runt domain to increase its affinity for DNA. The conserved ability of the Drosophila Runt protein to respond to the stimulating effect of mammalian PEBP2/CBF beta indicated that flies were likely to have a homologous beta protein. Using the yeast two-hybrid system to isolate cDNAs for Runt-interacting proteins, we identified two Drosophila genes, referred to as Brother and Big-brother, that have substantial sequence homology with PEBP2/CBF beta. Yeast two-hybrid experiments as well as in vitro DNA-binding studies confirmed the functional homology of the Brother, Big-brother, and PEBP2/CBF beta proteins and demonstrated that the conserved regions of the Runt and Brother proteins are required for their heterodimeric interaction. The DNA-bending properties of Runt domain proteins in the presence and absence of their partners were also examined. Our results show that Runt domain proteins bend DNA and that this bending is influenced by Brother protein family members, supporting the idea that heterodimerization is associated with a conformational change in the Runt domain. Analysis of expression patterns in Drosophila embryos revealed that Brother and Big-brother are likely to interact with runt in vivo and further suggested that the activity of these proteins is not restricted to their interaction with Runt.
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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.