ArticleNano letters2020
Geometrical Constraints Greatly Hinder Formin mDia1 Activity.
Article in Nano letters, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- The membrane-to-cortex distance regulates mDia1 activity to control cortical mechanics.Nature communications · 2026Article
- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- Article
- Fascin-induced bundling protects actin filaments from disassembly by cofilin.The Journal of cell biology · 2024Article
- Friction patterns guide actin network contraction.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- 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
- 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
- Cooperative bundling by fascin generates actin structures with architectures that depend on filament length.Frontiers in cell and developmental biology · 2022Article
- CYK-1/Formin activation in cortical RhoA signaling centers promotes organismal left-right symmetry breaking.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Actin filament oxidation by MICAL1 suppresses protections from cofilin-induced disassembly.EMBO reports · 2021Article
- F-Actin Cytoskeleton Network Self-Organization Through Competition and Cooperation.Annual review of cell and developmental biology · 2020Review
- The advantages of microfluidics to study actin biochemistry and biomechanics.Journal of muscle research and cell motility · 2020Review
Corrections and comments
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Formins are one of the central players in the assembly of most actin networks in cells. The sensitivity of these processive molecular machines to mechanical tension is now well established. However, how the activity of formins is affected by geometrical constraints related to network architecture, such as filament cross-linking and formin spatial confinement, remains largely unknown. Combining microfluidics and micropatterning, we reconstituted in vitro mDia1 formin-elongated filament bundles induced by fascin, with different geometrical constraints on the formins, and measured the impact of these constraints on formin elongation rate and processivity. When filaments are not bundled, the anchoring details of formins have only a mild impact on their processivity and do not affect their elongation rate. When formins are unanchored, we show that filament bundling by fascin reduces both their elongation rate and their processivity. Strikingly, when filaments elongated by surface-anchored formins are cross-linked together, formin elongation rate immediately decreases and processivity is reduced up to 24-fold depending on the cumulative impact of formin rotational and translational freedom. Our results reveal an unexpected crosstalk between the constraints at the filament and the formin levels. We anticipate that in cells the molecular details of formin anchoring to the plasma membrane strongly modulate formin activity at actin filament barbed ends.
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Registered trials
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.