ArticleMolecular and cellular biology1997
Meis proteins are major in vivo DNA binding partners for wild-type but not chimeric Pbx proteins.
Article in Molecular and cellular biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 110 papers.
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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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Who cites it
110 citing papers in PubMed, 256 citations in OpenAlex.
- TALE and Hox Transcription Factors Modulate Adult Behaviors in Zebrafish.Behavior genetics · 2026Article
- TALE and Hox Transcription Factors Control Adult Behaviors in Zebrafish.bioRxiv : the preprint server for biology · 2026Article
- RLS-associated MEIS transcription factors control distinct processes in human neural stem cells.Scientific reports · 2024Article
- Molecular basis of facilitated target search and sequence discrimination of TALE homeodomain transcription factor Meis1.Nature communications · 2024Article
- Spatial enhancer activation influences inhibitory neuron identity during mouse embryonic development.Nature neuroscience · 2024Article
- Mechanistic insights into cardiac regeneration and protection through MEIS inhibition.Turkish journal of biology = Turk biyoloji dergisi · 2024Article
- BREVIPEDICELLUS Positively Regulates Salt-Stress Tolerance inInternational journal of molecular sciences · 2023Article
- Transcription factors in microcephaly.Frontiers in neuroscience · 2023Review
- Research progress of PBX1 in developmental and regenerative medicine.International journal of medical sciences · 2023Review
- An insight into the diagnostic and prognostic value of HOX A13's expression in non-muscle invasive bladder cancer.Journal of clinical laboratory analysis · 2022Article
- Genetic Regulation of Vertebrate Forebrain Development by Homeobox Genes.Frontiers in neuroscience · 2022Review
- MEIS1 and its potential as a cancer therapeutic target (Review).International journal of molecular medicine · 2021Review
- The Hox protein conundrum: The "specifics" of DNA binding for Hox proteins and their partners.Developmental biology · 2021Review
- Assessing nucleic acid binding activity of four dinoflagellate cold shock domain proteins from Symbiodinium kawagutii and Lingulodinium polyedra.BMC molecular and cell biology · 2021Article
- Isoform-specific functions of an evolutionarily conserved 3 bp micro-exon alternatively spliced from another exon in Drosophila homothorax gene.Scientific reports · 2020Article
- Combinatorial action of NF-Y and TALE at embryonic enhancers defines distinct gene expression programs during zygotic genome activation in zebrafish.Developmental biology · 2020Article
- Oncogenic and tumor suppressor function of MEIS and associated factors.Turkish journal of biology = Turk biyoloji dergisi · 2020Article
- The human HOXA9 protein uses paralog-specific residues of the homeodomain to interact with TALE-class cofactors.Scientific reports · 2019Article
- Oligomeric self-association contributes to E2A-PBX1-mediated oncogenesis.Scientific reports · 2019Article
- A Hox-TALE regulatory circuit for neural crest patterning is conserved across vertebrates.Nature communications · 2019Article
50 more citing papers are in PubMed but not listed here.
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The Pbx1 and Meis1 proto-oncogenes code for divergent homeodomain proteins that are targets for oncogenic mutations in human and murine leukemias, respectively, and implicated by genetic analyses to functionally collaborate with Hox proteins during embryonic development and/or oncogenesis. Although Pbx proteins have been shown to dimerize with Hox proteins and modulate their DNA binding properties in vitro, the biochemical compositions of endogenous Pbx-containing complexes have not been determined. In the present study, we demonstrate that Pbx and Meis proteins form abundant complexes that comprise a major Pbx-containing DNA binding activity in nuclear extracts of cultured cells and mouse embryos. Pbx1 and Meis1 dimerize in solution and cooperatively bind bipartite DNA sequences consisting of directly adjacent Pbx and Meis half sites. Pbx1-Meis1 heterodimers display distinctive DNA binding specificities and cross-bind to a subset of Pbx-Hox sites, including those previously implicated as response elements for the execution of Pbx-dependent Hox programs in vivo. Chimeric oncoprotein E2a-Pbx1 is unable to bind DNA with Meis1, due to the deletion of amino-terminal Pbx1 sequences following fusion with E2a. We conclude that Meis proteins are preferred in vivo DNA binding partners for wild-type Pbx1, a relationship that is circumvented by its oncogenic counterpart E2a-Pbx1.
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