ArticleNature communications2017
mDia1 senses both force and torque during F-actin filament polymerization.
Article in Nature communications, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers.
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Who cites it
57 citing papers in PubMed.
- The membrane-to-cortex distance regulates mDia1 activity to control cortical mechanics.Nature communications · 2026Article
- Development and Characterization of a FRET-based Formin Tension Sensor in Living Cells.bioRxiv : the preprint server for biology · 2026Article
- Protein force spectroscopy using magnetic tweezers: Slow and steady wins the race?Biophysical journal · 2026Review
- Biophysical modeling identifies an optimal hybrid amoeboid-mesenchymal mechanism for maximal T cell migration speeds.Cell reports · 2026Article
- Translating Nature's Design Rules: How Catalysis and Life Science Guide Molecular Catassembly.JACS Au · 2026Review
- Actin cytoskeleton protection by the formin-mediated safety valve.Current opinion in cell biology · 2025Review
- Biophysical modeling identifies an optimal hybrid amoeboid-mesenchymal mechanism for maximal T cell migration speeds.bioRxiv : the preprint server for biology · 2025Article
- Genetically encoded mechano-sensors with versatile readouts and compact size.bioRxiv : the preprint server for biology · 2025Article
- Mechanisms of force transmission on cytokinesis Formin Cdc12 in fission yeast revealed by coiled-coil force sensors.bioRxiv : the preprint server for biology · 2025Article
- Real-time visualization reveals Mycobacterium tuberculosis ESAT-6 disrupts phagosome-like compartment via fibril-mediated vesiculation.Cell reports · 2025Article
- The mode of subunit addition regulates the processive elongation of actin filaments by formin.The Journal of biological chemistry · 2025Article
- Principles and regulation of mechanosensing.Journal of cell science · 2024Review
- Myosin forces elicit an F-actin structural landscape that mediates mechanosensitive protein recognition.bioRxiv : the preprint server for biology · 2024Article
- Multi-domain interaction mediated strength-building in human α-actinin dimers unveiled by direct single-molecule quantification.Nature communications · 2024Article
- Article
- Composite branched and linear F-actin maximize myosin-induced membrane shape changes in a biomimetic cell model.Communications biology · 2024Article
- Emergence of periodic circumferential actin cables from the anisotropic fusion of actin nanoclusters during tubulogenesis.Nature communications · 2024Article
- Modulation of E-Cadherin Function through the AmotL2 Isoforms Promotes Ameboid Cell Invasion.Cells · 2023Article
- Actin polymerisation and crosslinking drive left-right asymmetry in single cell and cell collectives.Nature communications · 2023Article
- Mechanisms underlying divergent relationships between CaThe Journal of physiology · 2023Article
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Authors and funding
11 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Formins, an important family of force-bearing actin-polymerizing factors, function as homodimers that bind with the barbed end of actin filaments through a ring-like structure assembled from dimerized FH2 domains. It has been hypothesized that force applied to formin may facilitate transition of the FH2 ring from an inhibitory closed conformation to a permissive open conformation, speeding up actin polymerization. We confirm this hypothesis for mDia1 dependent actin polymerization by stretching a single-actin filament in the absence of profilin using magnetic tweezers, and observe that increasing force from 0.5 to 10 pN can drastically speed up the actin polymerization rate. Further, we find that this force-promoted actin polymerization requires torsionally unconstrained actin filament, suggesting that mDia1 also senses torque. As actin filaments are subject to complex mechanical constraints in living cells, these results provide important insights into how formin senses these mechanical constraints and regulates actin organization accordingly.
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