ArticleNature communications2015
Calcium-controlled conformational choreography in the N-terminal half of adseverin.
Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
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Who cites it
10 citing papers in PubMed.
- A molecular perspective of gelsolin amyloidosis: An old foe with new faces.Cellular and molecular life sciences : CMLS · 2026Review
- Evaluation of genetic response of mesenchymal stem cells to nanosecond pulsed electric fields by whole transcriptome sequencing.World journal of stem cells · 2024Article
- Unlocking the potential of amorphous calcium carbonate: A star ascending in the realm of biomedical application.Acta pharmaceutica Sinica. B · 2024Review
- Scinderin Promotes Hydrogen Peroxide-induced Lens Epithelial Cell Injury in Age-related Cataract.Current molecular medicine · 2024Article
- A Myb enhancer-guided analysis of basophil and mast cell differentiation.Nature communications · 2022Article
- Identification of Ovarian Circular RNAs and Differential Expression Analysis between MeiShan and Large White Pigs.Animals : an open access journal from MDPI · 2020Article
- Novel inter-domain CaJournal of muscle research and cell motility · 2020Review
- The LC8-RavP ensemble Structure Evinces A Role for LC8 in Regulating Lyssavirus Polymerase Functionality.Journal of molecular biology · 2019Article
- Evolving SAXS versatility: solution X-ray scattering for macromolecular architecture, functional landscapes, and integrative structural biology.Current opinion in structural biology · 2019Review
- Molecular basis of a novel renal amyloidosis due to N184K gelsolin variant.Scientific reports · 2016Article
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Authors and funding
4 authors.
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Abstract
Adseverin is a member of the calcium-regulated gelsolin superfamily of actin-binding proteins. Here we report the crystal structure of the calcium-free N-terminal half of adseverin (iA1-A3) and the Ca(2+)-bound structure of A3, which reveal structural similarities and differences with gelsolin. Solution small-angle X-ray scattering combined with ensemble optimization revealed a dynamic Ca(2+)-dependent equilibrium between inactive, intermediate and active conformations. Increasing calcium concentrations progressively shift this equilibrium from a main population of inactive conformation to the active form. Molecular dynamics simulations of iA1-A3 provided insights into Ca(2+)-induced destabilization, implicating a critical role for the A2 type II calcium-binding site and the A2A3 linker in the activation process. Finally, mutations that disrupt the A1/A3 interface increase Ca(2+)-independent F-actin severing by A1-A3, albeit at a lower efficiency than observed for gelsolin domains G1-G3. Together, these data address the calcium dependency of A1-A3 activity in relation to the calcium-independent activity of G1-G3.
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