ArticleNature communications2013
Formin mDia1 senses and generates mechanical forces on actin filaments.
Article in Nature communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 126 papers.
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Who cites it
126 citing papers in PubMed, 223 citations in OpenAlex.
- Myosin II-independent contraction of actin filaments in membrane nanotubes.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Inorganic phosphate rapidly switches the stability of Arp2/3-induced actin branches.The Journal of cell biology · 2026Article
- 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
- Impact of N-terminal dimerization on formin homology 1 domain polymer dynamics and actin assembly.Biophysical journal · 2026Article
- Maintaining Genome Integrity: Actin Polymerization Stabilizes Chromatin Bridges in Cytokinesis.International journal of molecular sciences · 2026Review
- Actin cytoskeleton protection by the formin-mediated safety valve.Current opinion in cell biology · 2025Review
- Genetically encoded mechano-sensors with versatile readouts and compact size.bioRxiv : the preprint server for biology · 2025Article
- Protrusion-Derived Extracellular Vesicles (PD-EVs) and Their Diverse Origins: Key Players in Cellular Communication, Cancer Progression, and T Cell Modulation.Biology of the cell · 2025Review
- Making cells inter-connected for signaling communication: a developmental view of cytonemes.Cell communication and signaling : CCS · 2025Review
- Mechanisms of force transmission on cytokinesis Formin Cdc12 in fission yeast revealed by coiled-coil force sensors.bioRxiv : the preprint server for biology · 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
- Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.The Journal of cell biology · 2024Article
- Myosin forces elicit an F-actin structural landscape that mediates mechanosensitive protein recognition.bioRxiv : the preprint server for biology · 2024Article
- Composite branched and linear F-actin maximize myosin-induced membrane shape changes in a biomimetic cell model.Communications biology · 2024Article
- Coordination of actin plus-end dynamics by IQGAP1, formin, and capping protein.bioRxiv : the preprint server for biology · 2024Article
- Regeneration of actin filament branches from the same Arp2/3 complex.Science advances · 2024Article
- Improved Prediction of Molecular Response to Pulling by Combining Force Tempering with Replica Exchange Methods.The journal of physical chemistry. B · 2024Article
- Emergence of periodic circumferential actin cables from the anisotropic fusion of actin nanoclusters during tubulogenesis.Nature communications · 2024Article
66 more citing papers are in PubMed but not listed here.
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cytoskeleton assembly is instrumental in the regulation of biological functions by physical forces. In a number of key cellular processes, actin filaments elongated by formins such as mDia are subject to mechanical tension, yet how mechanical forces modulate the assembly of actin filaments is an open question. Here, using the viscous drag of a microfluidic flow, we apply calibrated piconewton pulling forces to individual actin filaments that are being elongated at their barbed end by surface-anchored mDia1 proteins. We show that mDia1 is mechanosensitive and that the elongation rate of filaments is increased up to two-fold by the application of a pulling force. We also show that mDia1 is able to track a depolymerizing barbed end in spite of an opposing pulling force, which means that mDia1 can efficiently put actin filaments under mechanical tension. Our findings suggest that formin function in cells is tightly coupled to the mechanical activity of other machineries.
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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.