ArticleProceedings of the National Academy of Sciences of the United States of America1997
The LIM-domain binding protein Ldb1 and its partner LMO2 act as negative regulators of erythroid differentiation.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 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
67 citing papers in PubMed, 157 citations in OpenAlex.
- Cytoplasmic LIM domain only 2 enhances tumor endothelial cell migration through integrin β1-mediated focal adhesion signaling.Acta neuropathologica communications · 2026Article
- Single-stranded DNA-binding proteins are essential components of the architectural LDB1 protein complex.Molecular cell · 2025Article
- A Novel Effect of Id2 in Microglia TNFα Regulation.Molecular neurobiology · 2025Article
- An intricate regulatory circuit between FLI1 and GATA1/GATA2/LDB1/ERG dictates erythroid vs. megakaryocytic differentiation.Molecular medicine reports · 2024Article
- The transcription factor complex LMO2/TAL1 regulates branching and endothelial cell migration in sprouting angiogenesis.Scientific reports · 2022Article
- SuperDendrix algorithm integrates genetic dependencies and genomic alterations across pathways and cancer types.Cell genomics · 2022Article
- Article
- Genome-Wide Association Study of Body Weight Traits in Inner Mongolia Cashmere Goats.Frontiers in veterinary science · 2021Article
- The transcription factor TAL1 and miR-17-92 create a regulatory loop in hematopoiesis.Scientific reports · 2020Article
- Article
- Beadex, a homologue of the vertebrate LIM domain only protein, is a novel regulator of crystal cell development inJournal of genetics · 2019Article
- miR-9 upregulation leads to inhibition of erythropoiesis by repressing FoxO3.Scientific reports · 2018Article
- Article
- Compensatory Actions of Ldb Adaptor Proteins During Corticospinal Motor Neuron Differentiation.Cerebral cortex (New York, N.Y. : 1991) · 2017Article
- Cofactors of LIM Domains Associate with Estrogen Receptor α to Regulate the Expression of Noncoding RNA H19 and Corneal Epithelial Progenitor Cell Function.The Journal of biological chemistry · 2016Article
- The LMO2 oncogene regulates DNA replication in hematopoietic cells.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- LMO2 at 25 years: a paradigm of chromosomal translocation proteins.Open biology · 2015Review
- LMO4 functions as a negative regulator of sensory organ formation in the mammalian cochlea.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014Article
- The co-factor of LIM domains (CLIM/LDB/NLI) maintains basal mammary epithelial stem cells and promotes breast tumorigenesis.PLoS genetics · 2014Article
7 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The nuclear LIM domain protein LMO2, a T cell oncoprotein, is essential for embryonic erythropoiesis. LIM-only proteins are presumed to act primarily through protein-protein interactions. We, and others, have identified a widely expressed protein, Ldb1, whose C-terminal 76-residues are sufficient to mediate interaction with LMO2. In murine erythroleukemia cells, the endogenous Lbd1 and LMO2 proteins exist in a stable complex, whose binding affinity appears greater than that between LMO2 and the bHLH transcription factor SCL. However, Ldb1, LMO2, and SCL/E12 can assemble as a multiprotein complex on a consensus SCL binding site. Like LMO2, the Ldb1 gene is expressed in fetal liver and erythroid cell lines. Forced expression of Ldb1 in G1ER proerythroblast cells inhibited cellular maturation, a finding compatible with the decrease in Ldb1 gene expression that normally occurs during erythroid differentiation. Overexpression of the LMO2 gene also inhibited erythroid differentiation. Our studies demonstrate a function for Ldb1 in hemopoietic cells and suggest that one role of the Ldb1/LMO2 complex is to maintain erythroid precursors in an immature state.
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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.