ArticleJournal of the American Chemical Society2023
Force-Dependent Structural Changes of Filamin C Rod Domains Regulated by Filamin C Dimer.
Article in Journal of the American Chemical Society, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
What it found
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Who cites it
9 citing papers in PubMed, 17 citations in OpenAlex.
- Endothelial Filamin C Alleviates Atherosclerosis via PINK1/Parkin-Dependent Mitophagy and mtDNA-cGAS-STING Inflammation Suppression.Journal of cardiovascular development and disease · 2026Article
- Tissue-specific epigenetic regulation of fat metabolism in pigs through integrated analysis of DNA methylation and gene expression networks.Journal of animal science and biotechnology · 2026Article
- Identification of novel and known variants inFrontiers in cardiovascular medicine · 2026Article
- Single-molecule tweezers decode hidden dimerization patterns of membrane proteins within lipid bilayers.Nature communications · 2025Article
- Decoding force-transmission linkages for therapeutic targeting and engineering.APL bioengineering · 2025Review
- Biomaterials Mimicking Mechanobiology: A Specific Design for a Specific Biological Application.International journal of molecular sciences · 2024Review
- Multi-domain interaction mediated strength-building in human α-actinin dimers unveiled by direct single-molecule quantification.Nature communications · 2024Article
- Determination of single-molecule loading rate during mechanotransduction in cell adhesion.Science (New York, N.Y.) · 2024Article
- The Role of Mechanotransduction in Contact Inhibition of Locomotion and Proliferation.International journal of molecular sciences · 2024Review
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Filamin C (FLNC), a large dimeric actin-binding protein in muscle cells, plays a critical role in transmitting force in the cytoskeleton and that between membrane receptors and the cytoskeleton. It performs crucial mechanosensing and downstream mechanotransduction functions via force-dependent interactions with signaling proteins. Mutations in FLNC have been linked to muscle and heart diseases. The mechanical responses of the force-bearing elements in FLNC have not been determined. This study investigated the mechanical responses of FLNC domains and their dimerization interface using magnetic tweezers. Results showed high stability of the N-terminal domains in the rod-1 segment but significant changes in the rod-2 domains in response to forces of a few piconewtons (pN). The dimerization interface, formed by the R24 domain, has a lifetime of seconds to tens of seconds at pN forces, and it dissociates within 1 s at forces greater than 14 pN. The findings suggest the FLNC dimerization interface provides sufficient mechanical stability that enables force-dependent structural changes in rod-2 domains for signaling protein binding and maintains structural integrity of the rod-1 domains.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.