ArticleBiophysical journal2017
Biphasic Effect of Profilin Impacts the Formin mDia1 Force-Sensing Mechanism in Actin Polymerization.
Article in Biophysical journal, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.
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Who cites it
22 citing papers in PubMed, 42 citations in OpenAlex.
- Actin cytoskeleton protection by the formin-mediated safety valve.Current opinion in cell biology · 2025Review
- Optogenetic actin network assembly on lipid bilayer uncovers the network density-dependent functions of actin-binding proteins.Nature communications · 2025Article
- The mode of subunit addition regulates the processive elongation of actin filaments by formin.The Journal of biological chemistry · 2025Article
- Direct observation of the conformational states of formin mDia1 at actin filament barbed ends and along the filament.Molecular biology of the cell · 2023Article
- Biochemical and mechanical regulation of actin dynamics.Nature reviews. Molecular cell biology · 2022Review
- Rapid assembly of a polar network architecture drives efficient actomyosin contractility.Cell reports · 2022Article
- Celebrating 20 years of live single-actin-filament studies with five golden rules.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Profilin and Mical combine to impair F-actin assembly and promote disassembly and remodeling.Nature communications · 2021Article
- Tug-of-war between actomyosin-driven antagonistic forces determines the positioning symmetry in cell-sized confinement.Nature communications · 2020Article
- Cancer Cells Resist Mechanical Destruction in Circulation via RhoA/Actomyosin-Dependent Mechano-Adaptation.Cell reports · 2020Article
- The advantages of microfluidics to study actin biochemistry and biomechanics.Journal of muscle research and cell motility · 2020Review
- Geometrical Constraints Greatly Hinder Formin mDia1 Activity.Nano letters · 2020Article
- Thermodynamically consistent treatment of the growth of a biopolymer in the presence of a smooth obstacle interaction potential.Physical review. E · 2019Article
- Simultaneous Quantification of the Interplay Between Molecular Turnover and Cell Mechanics by AFM-FRAP.Small (Weinheim an der Bergstrasse, Germany) · 2019Article
- New insights into cytoskeletal remodeling during platelet production.Journal of thrombosis and haemostasis : JTH · 2019Review
- Mechanisms of formin-mediated actin assembly and dynamics.Biophysical reviews · 2018Review
- Article
- Ependymal cilia beating induces an actin network to protect centrioles against shear stress.Nature communications · 2018Article
- Computational modeling highlights the role of the disordered Formin Homology 1 domain in profilin-actin transfer.FEBS letters · 2018Article
- Article
Corrections and comments
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Authors and funding
6 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formins are force-sensing proteins that regulate actin polymerization dynamics. Here, we applied stretching tension to individual actin filaments under the regulation of formin mDia1 to investigate the mechanical responses in actin polymerization dynamics. We found that the elongation of an actin filament was accelerated to a greater degree by stretching tension for ADP-G-actin than that for ATP-G-actin. An apparent decrease in the critical concentration of G-actin was observed, especially in ADP-G-actin. These results on two types of G-actin were reproduced by a simple kinetic model, assuming the rapid equilibrium between pre- and posttranslocated states of the formin homology domain two dimer. In addition, profilin concentration dramatically altered the force-dependent acceleration of actin filament elongation, which ranged from twofold to an all-or-none response. Even under conditions in which actin depolymerization occurred, applications of a several-piconewton stretching tension triggered rapid actin filament elongation. This extremely high force-sensing mechanism of mDia1 and profilin could be explained by the force-dependent coordination of the biphasic effect of profilin; i.e., an acceleration effect masked by a depolymerization effect became dominant under stretching tension, negating the latter to rapidly enhance the elongation rate. Our findings demonstrate that the biphasic effect of profilin is controlled by mechanical force, thus expanding the function of mDia1 as a mechanosensitive regulator of actin polymerization.
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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.