ArticleThe Journal of biological chemistry2013
A structural basis for the regulation of the LIM-homeodomain protein islet 1 (Isl1) by intra- and intermolecular interactions.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed, 26 citations in OpenAlex.
- Alternative LIM homeodomain splice variants are dynamically regulated at key developmental steps in vertebrates.Developmental dynamics : an official publication of the American Association of Anatomists · 2022Article
- Phosphorylation of islet-1 serine 269 by CDK1 increases its transcriptional activity and promotes cell proliferation in gastric cancer.Molecular medicine (Cambridge, Mass.) · 2021Article
- Structural and functional analysis of LIM domain-dependent recruitment of paxillin to αvβ3 integrin-positive focal adhesions.Communications biology · 2021Article
- Bioinformatic Analysis of Structure and Function of LIM Domains of Human Zyxin Family Proteins.International journal of molecular sciences · 2021Article
- Spotlight on Isl1: A Key Player in Cardiovascular Development and Diseases.Frontiers in cell and developmental biology · 2021Review
- Crystal structure of human LDB1 in complex with SSBP2.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Towards a Central Role ofGenes · 2018Article
- Interactions between LHX3- and ISL1-family LIM-homeodomain transcription factors are conserved in Caenorhabditis elegans.Scientific reports · 2017Article
- Differential methylation of genes in individuals exposed to maternal diabetes in utero.Diabetologia · 2017Article
- Priorities and trends in the study of proteins in eye research, 1924-2014.Proteomics. Clinical applications · 2015Article
- Functional Diversification of Motor Neuron-specific Isl1 Enhancers during Evolution.PLoS genetics · 2015Article
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7 authors at 1 institution in 1 country.
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Abstract
Islet 1 (Isl1) is a transcription factor of the LIM-homeodomain (LIM-HD) protein family and is essential for many developmental processes. LIM-HD proteins all contain two protein-interacting LIM domains, a DNA-binding homeodomain (HD), and a C-terminal region. In Isl1, the C-terminal region also contains the LIM homeobox 3 (Lhx3)-binding domain (LBD), which interacts with the LIM domains of Lhx3. The LIM domains of Isl1 have been implicated in inhibition of DNA binding potentially through an intramolecular interaction with or close to the HD. Here we investigate the LBD as a candidate intramolecular interaction domain. Competitive yeast-two hybrid experiments indicate that the LIM domains and LBD from Isl1 can interact with apparently low affinity, consistent with no detection of an intermolecular interaction in the same system. Nuclear magnetic resonance studies show that the interaction is specific, whereas substitution of the LBD with peptides of the same amino acid composition but different sequence is not specific. We solved the crystal structure of a similar but higher affinity complex between the LIM domains of Isl1 and the LIM interaction domain from the LIM-HD cofactor protein LIM domain-binding protein 1 (Ldb1) and used these coordinates to generate a homology model of the intramolecular interaction that indicates poorer complementarity for the weak intramolecular interaction. The intramolecular interaction in Isl1 may provide protection against aggregation, minimize unproductive DNA binding, and facilitate cofactor exchange within the cell.
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