ArticleBiophysical journal2014
Quantitation of the calcium and membrane binding properties of the C2 domains of dysferlin.
Article in Biophysical journal, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.
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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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Who cites it
38 citing papers in PubMed, 65 citations in OpenAlex.
- Dysferlin and the Regulation of CaCells · 2025Review
- Structural insights into lipid membrane binding by human ferlins.The EMBO journal · 2025Article
- Syntaxin 4-enhanced plasma membrane repair is independent of dysferlin in skeletal muscle.American journal of physiology. Cell physiology · 2025Article
- Gene-editing in patient and humanized-mice primary muscle stem cells rescues dysferlin expression in dysferlin-deficient muscular dystrophy.Nature communications · 2025Article
- Whole Exome Sequencing Identified a Stop-Gained Mutation in DYSF Gene Associated With Dysferlinopathy in an Iranian Family.International journal of genomics · 2025Article
- Cryo-EM structures of the membrane repair protein dysferlin.Nature communications · 2024Article
- Comprehensive Proteomic Analysis of Dysferlinopathy Unveiling Molecular Mechanisms and Biomarkers Linked to Pathological Progression.CNS neuroscience & therapeutics · 2024Article
- Limb Girdle Muscular Dystrophy Type 2B (LGMD2B): Diagnosis and Therapeutic Possibilities.International journal of molecular sciences · 2024Review
- The Dysferlinopathies Conundrum: Clinical Spectra, Disease Mechanism and Genetic Approaches for Treatments.Biomolecules · 2024Review
- Pharmacotherapeutic Approaches to Treatment of Muscular Dystrophies.Biomolecules · 2023Review
- The Dysferlin C2A Domain Binds PI(4,5)P2 and Penetrates Membranes.Journal of molecular biology · 2023Article
- Role of calcium-sensor proteins in cell membrane repair.Bioscience reports · 2023Review
- The C2 domains of dysferlin: roles in membrane localization, CaThe Journal of physiology · 2022Article
- 4-Phenylbutyrate restores localization and membrane repair to human dysferlin mutations.iScience · 2022Article
- Elevated CaFrontiers in physiology · 2022Article
- Redefining the architecture of ferlin proteins: Insights into multi-domain protein structure and function.PloS one · 2022Article
- Truncation of the otoferlin transmembrane domain alters the development of hair cells and reduces membrane docking.Molecular biology of the cell · 2021Article
- Annexins and Membrane Repair Dysfunctions in Muscular Dystrophies.International journal of molecular sciences · 2021Review
- Ferlins and TgDOC2 inLife (Basel, Switzerland) · 2021Article
- Sarcolemma wounding activates dynamin-dependent endocytosis in striated muscle.The FEBS journal · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Dysferlin is a large membrane protein involved in calcium-triggered resealing of the sarcolemma after injury. Although it is generally accepted that dysferlin is Ca(2+) sensitive, the Ca(2+) binding properties of dysferlin have not been characterized. In this study, we report an analysis of the Ca(2+) and membrane binding properties of all seven C2 domains of dysferlin as well as a multi-C2 domain construct. Isothermal titration calorimetry measurements indicate that all seven dysferlin C2 domains interact with Ca(2+) with a wide range of binding affinities. The C2A and C2C domains were determined to be the most sensitive, with Kd values in the tens of micromolar, whereas the C2D domain was least sensitive, with a near millimolar Kd value. Mutagenesis of C2A demonstrates the requirement for negatively charged residues in the loop regions for divalent ion binding. Furthermore, dysferlin displayed significantly lower binding affinity for the divalent cations magnesium and strontium. Measurement of a multidomain construct indicates that the solution binding affinity does not change when C2 domains are linked. Finally, sedimentation assays suggest all seven C2 domains bind lipid membranes, and that Ca(2+) enhances but is not required for interaction. This report reveals for the first time, to our knowledge, that all dysferlin domains bind Ca(2+) albeit with varying affinity and stoichiometry.
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Registered trials
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