ArticleFEBS letters2018
Computational modeling highlights the role of the disordered Formin Homology 1 domain in profilin-actin transfer.
Article in FEBS letters, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 34 citations in OpenAlex.
- Titin's Intrinsically Disordered PEVK Domain Modulates Actin Polymerization.International journal of molecular sciences · 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
- Actin filament dynamics at barbed ends: New structures, new insights.Current opinion in cell biology · 2024Review
- Exploring the Role of the Plant Actin Cytoskeleton: From Signaling to Cellular Functions.International journal of molecular sciences · 2023Review
- The proline-rich domain of fission yeast WASp (Wsp1p) interacts with actin filaments and inhibits actin polymerization.FEBS letters · 2023Article
- Steps of actin filament branch formation by Arp2/3 complex investigated with coarse-grained molecular dynamics.Frontiers in cell and developmental biology · 2023Article
- A structural model of the profilin-formin pacemaker system for actin filament elongation.Scientific reports · 2022Article
- Alterations to the broad-spectrum formin inhibitor SMIFH2 modulate potency but not specificity.Scientific reports · 2022Article
- Article
- The Actin Regulators Involved in the Function and Related Diseases of Lymphocytes.Frontiers in immunology · 2022Review
- Nucleation limits the lengths of actin filaments assembled by formin.Biophysical journal · 2021Article
- Article
- Profilin's Affinity for Formin Regulates the Availability of Filament Ends for Actin Monomer Binding.Journal of molecular biology · 2020Article
- Insights into Actin Polymerization and Nucleation Using a Coarse-Grained Model.Biophysical journal · 2020Article
- Competition for delivery of profilin-actin to barbed ends limits the rate of formin-mediated actin filament elongation.The Journal of biological chemistry · 2020Article
- Geometrical Constraints Greatly Hinder Formin mDia1 Activity.Nano letters · 2020Article
- Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020Article
- Mechanisms of formin-mediated actin assembly and dynamics.Biophysical reviews · 2018Review
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Formins accelerate actin polymerization, assumed to occur through flexible Formin Homology 1 (FH1) domain-mediated transfer of profilin-actin to the barbed end. To study FH1 properties and address sequence effects, including varying length/distribution of profilin-binding proline-rich motifs, we performed all-atom simulations of a set of representative FH1 domains of formins: mouse mDia1 and mDia2, budding yeast Bni1 and Bnr1, and fission yeast Cdc12, For3, and Fus1. We find FH1 has flexible regions between high-propensity polyproline helix regions. A coarse-grained model retaining sequence specificity, assuming rigid polyproline segments, describes their size. Multiple bound profilins or profilin-actin complexes expand mDia1-FH1, which may be important in cells. Simulations of the barbed end bound to Bni1-FH1-FH2 dimer show that the leading FH1 can better transfer profilin or profilin-actin, with decreasing probability as the distance from FH2 increases.
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