ArticleCytoskeleton (Hoboken, N.J.)2019
Crosslinking actin networks produces compressive force.
Article in Cytoskeleton (Hoboken, N.J.), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed.
- Fast Actin Disassembly and Fimbrin Mechanosensitivity Support Rapid Turnover in a Model of Clathrin-Mediated Endocytosis.Cytoskeleton (Hoboken, N.J.) · 2025Article
- Dynamic remodeling of actin networks by cyclase-associated protein and CAP-Abp1 complexes.Current biology : CB · 2023Article
- Article
- Endocytosis against high turgor pressure is made easier by partial coating and freely rotating base.Biophysical journal · 2021Article
- Biophysical forces in membrane bending and traffic.Current opinion in cell biology · 2020Review
- Single-molecule turnover dynamics of actin and membrane coat proteins in clathrin-mediated endocytosis.eLife · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Actin has been shown to be essential for clathrin-mediated endocytosis in yeast. However, actin polymerization alone is likely insufficient to produce enough force to deform the membrane against the huge turgor pressure of yeast cells. In this paper, we used Brownian dynamics simulations to demonstrate that crosslinking of a meshwork of nonpolymerizing actin filaments is able to produce compressive forces. We show that the force can be up to several thousand pico-Newtons if the crosslinker has a high stiffness. The force decays over time as a result of crosslinker turnover, and is a result of converting chemical binding energy into elastic energy.
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Registered trials
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