ArticleThe Journal of biological chemistry2011
Structural basis for partial redundancy in a class of transcription factors, the LIM homeodomain proteins, in neural cell type specification.
Article in The Journal of biological chemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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Who cites it
27 citing papers in PubMed, 39 citations in OpenAlex.
- Drug Repurposing for Targeting ISL LIM Homeobox 2 in Treatment of Endometriosis: A Computational Study.International journal of fertility & sterility · 2025Article
- Lhx4 surpasses its paralog Lhx3 in promoting the differentiation of spinal V2a interneurons.Cellular and molecular life sciences : CMLS · 2024Article
- TheFrontiers in endocrinology · 2023Article
- Intrinsically disordered regions of tristetraprolin and DCP2 directly interact to mediate decay of ARE-mRNA.Nucleic acids research · 2022Article
- Contrasting DNA-binding behaviour by ISL1 and LHX3 underpins differential gene targeting in neuronal cell specification.Journal of structural biology: X · 2021Article
- A patient with combined pituitary hormone deficiency and osteogenesis imperfecta associated with mutations inJournal of advanced research · 2020Article
- Disparate binding kinetics by an intrinsically disordered domain enables temporal regulation of transcriptional complex formation.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Article
- Interactions between LHX3- and ISL1-family LIM-homeodomain transcription factors are conserved in Caenorhabditis elegans.Scientific reports · 2017Article
- Selecting optimal combinations of transcription factors to promote axon regeneration: Why mechanisms matter.Neuroscience letters · 2017Review
- LIM domain-binding 1 maintains the terminally differentiated state of pancreatic β cells.The Journal of clinical investigation · 2017Article
- ISL1-based LIM complexes control Slit2 transcription in developing cranial motor neurons.Scientific reports · 2016Article
- Functional Diversification of Motor Neuron-specific Isl1 Enhancers during Evolution.PLoS genetics · 2015Article
- Slit and Semaphorin signaling governed by Islet transcription factors positions motor neuron somata within the neural tube.Experimental neurology · 2015Article
- Alternative splicing of the LIM-homeodomain transcription factor Isl1 in the mouse retina.Molecular and cellular neurosciences · 2015Article
- Lhx3 and Lhx4 suppress Kolmer-Agduhr interneuron characteristics within zebrafish axial motoneurons.Development (Cambridge, England) · 2014Article
- Biophysical properties of intrinsically disordered p130Cas substrate domain--implication in mechanosensing.PLoS computational biology · 2014Article
- Article
- A structural basis for the regulation of the LIM-homeodomain protein islet 1 (Isl1) by intra- and intermolecular interactions.The Journal of biological chemistry · 2013Article
- Linkers in the structural biology of protein-protein interactions.Protein science : a publication of the Protein Society · 2013Review
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Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Combinations of LIM homeodomain proteins form a transcriptional "LIM code" to direct the specification of neural cell types. Two paralogous pairs of LIM homeodomain proteins, LIM homeobox protein 3/4 (Lhx3/Lhx4) and Islet-1/2 (Isl1/Isl2), are expressed in developing ventral motor neurons. Lhx3 and Isl1 interact within a well characterized transcriptional complex that triggers motor neuron development, but it was not known whether Lhx4 and Isl2 could participate in equivalent complexes. We have identified an Lhx3-binding domain (LBD) in Isl2 based on sequence homology with the Isl1(LBD) and show that both Isl2(LBD) and Isl1(LBD) can bind each of Lhx3 and Lhx4. X-ray crystal- and small-angle x-ray scattering-derived solution structures of an Lhx4·Isl2 complex exhibit many similarities with that of Lhx3·Isl1; however, structural differences supported by mutagenic studies reveal differences in the mechanisms of binding. Differences in binding have implications for the mode of exchange of protein partners in transcriptional complexes and indicate a divergence in functions of Lhx3/4 and Isl1/2. The formation of weaker Lhx·Isl complexes would likely be masked by the availability of the other Lhx·Isl complexes in postmitotic motor neurons.
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