ArticleThe Journal of biological chemistry2008
Distinct roles of beta1 metal ion-dependent adhesion site (MIDAS), adjacent to MIDAS (ADMIDAS), and ligand-associated metal-binding site (LIMBS) cation-binding sites in ligand recognition by integrin alpha2beta1.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed, 61 citations in OpenAlex.
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- Integrins mediate symbiont-specific uptake in cnidarian larvae.EMBO reports · 2026Article
- An RGD motif on SARS-CoV-2 Spike induces TGF-β signaling and downregulates interferon.Journal of virology · 2025Article
- MnBiophysical journal · 2025Article
- The Force-Dependent Mechanism of an Integrin α4β7-MAdCAM-1 Interaction.International journal of molecular sciences · 2023Article
- Structural analysis of peptide binding to integrins for cancer detection and treatment.Biophysical reviews · 2023Review
- Cryo-EM structures of full-length integrin αIIbβ3 in native lipids.Nature communications · 2023Article
- The C-type lectin domain of CD62P (P-selectin) functions as an integrin ligand.Life science alliance · 2023Article
- INTEGRINS: A BEDSIDE TO BENCH TO BEDSIDE STORY.Transactions of the American Clinical and Climatological Association · 2023Article
- Junctional epithelium and hemidesmosomes: Tape and rivets for solving the "percutaneous device dilemma" in dental and other permanent implants.Bioactive materials · 2022Review
- Regulation of integrin α5β1 conformational states and intrinsic affinities by metal ions and the ADMIDAS.Molecular biology of the cell · 2022Article
- Structural, biochemical, and functional properties of the Rap1-Interacting Adaptor Molecule (RIAM).Biomedical journal · 2022Review
- β2 Integrins-Multi-Functional Leukocyte Receptors in Health and Disease.International journal of molecular sciences · 2020Review
- Phagocytic Integrins: Activation and Signaling.Frontiers in immunology · 2020Review
- A three-way inter-molecular network accounts for the CaThe Journal of biological chemistry · 2018Article
- Magnetic Resonance Imaging of Atherosclerotic Plaque at Clinically Relevant Field Strengths (1T) by Targeting the Integrin α4β1.Scientific reports · 2018Article
- Intrinsic local destabilization of the C-terminus predisposes integrin α1 I domain to a conformational switch induced by collagen binding.Protein science : a publication of the Protein Society · 2016Article
- Slingshot-Cofilin activation mediates mitochondrial and synaptic dysfunction via Aβ ligation to β1-integrin conformers.Cell death and differentiation · 2015Article
- The α-subunit regulates stability of the metal ion at the ligand-associated metal ion-binding site in β3 integrins.The Journal of biological chemistry · 2014Article
- Variation in one residue associated with the metal ion-dependent adhesion site regulates αIIbβ3 integrin ligand binding affinity.PloS one · 2013Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Integrin-ligand interactions are regulated in a complex manner by divalent cations, and previous studies have identified ligand-competent, stimulatory, and inhibitory cation-binding sites. In collagen-binding integrins, such as alpha2beta1, ligand recognition takes place exclusively at the alpha subunit I domain. However, activation of the alphaI domain depends on its interaction with a structurally similar domain in the beta subunit known as the I-like or betaI domain. The top face of the betaI domain contains three cation-binding sites: the metal-ion dependent adhesion site (MIDAS), the ADMIDAS (adjacent to MIDAS), and LIMBS (ligand-associated metal-binding site). The role of these sites in controlling ligand binding to the alphaI domain has yet to be elucidated. Mutation of the MIDAS or LIMBS completely blocked collagen binding to alpha2beta1; in contrast mutation of the ADMIDAS reduced ligand recognition but this effect could be overcome by the activating monoclonal antibody TS2/16. Hence, the MIDAS and LIMBS appear to be essential for the interaction between alphaI and betaI, whereas occupancy of the ADMIDAS has an allosteric effect on the conformation of betaI. An activating mutation in the alpha2 I domain partially restored ligand binding to the MIDAS and LIMBS mutants. Analysis of the effects of Ca(2+), Mg(2+), and Mn(2+) on ligand binding to these mutants showed that the MIDAS is a ligand-competent site through which Mn(2+) stimulates ligand binding, whereas the LIMBS is a stimulatory Ca(2+)-binding site, occupancy of which increases the affinity of Mg(2+) for the MIDAS.
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