ArticleeLife2018
Gating mechanisms during actin filament elongation by formins.
Article in eLife, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed.
- Development and Characterization of a FRET-based Formin Tension Sensor in Living Cells.bioRxiv : the preprint server for biology · 2026Article
- Enhanced Exploration of Protein Conformational Space through Integration of Ultra-Coarse-Grained Models to Multiscale Workflows.The journal of physical chemistry. B · 2025Article
- Molecular mechanism of Arp2/3 complex activation by nucleation-promoting factors and an actin monomer.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- FHOD-1 and profilin protect sarcomeres against contraction-induced deformation> inMolecular biology of the cell · 2024Article
- Prediction of the essential intermolecular contacts for side-binding of VASP on F-actin.Cytoskeleton (Hoboken, N.J.) · 2024Article
- The DIAPH3 linker specifies a β-actin network that maintains RhoA and Myosin-II at the cytokinetic furrow.Nature communications · 2024Article
- FHOD-1/profilin-mediated actin assembly protects sarcomeres against contraction-induced deformation inbioRxiv : the preprint server for biology · 2024Article
- Direct observation of the conformational states of formin mDia1 at actin filament barbed ends and along the filament.Molecular biology of the cell · 2023Article
- Actin assembly requirements of the formin Fus1 to build the fusion focus.Journal of cell science · 2022Article
- Visualizing molecules of functionaleLife · 2022Article
- Biochemical characterization of actin assembly mechanisms with ALS-associated profilin variants.European journal of cell biology · 2022Article
- Cooperative bundling by fascin generates actin structures with architectures that depend on filament length.Frontiers in cell and developmental biology · 2022Article
- Nucleation limits the lengths of actin filaments assembled by formin.Biophysical journal · 2021Article
- The formin inhibitor SMIFH2 inhibits members of the myosin superfamily.Journal of cell science · 2021Article
- Formin homology domains of Daam1 bind to Fascin and collaboratively promote pseudopodia formation and cell migration in breast cancer.Cell proliferation · 2021Article
- Towards a structural understanding of the remodeling of the actin cytoskeleton.Seminars in cell & developmental biology · 2020Review
- Competition for delivery of profilin-actin to barbed ends limits the rate of formin-mediated actin filament elongation.The Journal of biological chemistry · 2020Article
- Article
- Control of actin dynamics during cell motility.F1000Research · 2019Review
- Mechanisms of formin-mediated actin assembly and dynamics.Biophysical reviews · 2018Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Formins play an important role in the polymerization of unbranched actin filaments, and particular formins slow elongation by 5-95%. We studied the interactions between actin and the FH2 domains of formins Cdc12, Bni1 and mDia1 to understand the factors underlying their different rates of polymerization. All-atom molecular dynamics simulations revealed two factors that influence actin filament elongation and correlate with the rates of elongation. First, FH2 domains can sterically block the addition of new actin subunits. Second, FH2 domains flatten the helical twist of the terminal actin subunits, making the end less favorable for subunit addition. Coarse-grained simulations over longer time scales support these conclusions. The simulations show that filaments spend time in states that either allow or block elongation. The rate of elongation is a time-average of the degree to which the formin compromises subunit addition rather than the formin-actin complex literally being in 'open' or 'closed' states.
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Registered trials
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