ArticleJournal of molecular biology2013
Molecular origins of cofilin-linked changes in actin filament mechanics.
Article in Journal of molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.
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Who cites it
32 citing papers in PubMed, 47 citations in OpenAlex.
- Deciphering the Cofilin Oligomers via Intermolecular Disulfide Bond Formation: A Coarse-Grained Molecular Dynamics Approach to Understanding Cofilin's Regulation on Actin Filaments.The journal of physical chemistry. B · 2024Article
- The role of actin cytoskeleton CFL1 and ADF/cofilin superfamily in inflammatory response.Frontiers in molecular biosciences · 2024Review
- Cooperative ligand binding to a double-stranded Ising lattice-Application to cofilin binding to actin filaments.PNAS nexus · 2023Article
- Twist response of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Molecular and structural basis of actin filament severing by ADF/cofilin.Computational and structural biotechnology journal · 2022Article
- Molecular dynamics study of water channels in natural and synthetic amyloid-β fibrils.The Journal of chemical physics · 2021Article
- Clusters of a Few Bound Cofilins Sever Actin Filaments.Journal of molecular biology · 2021Article
- Catastrophic actin filament bursting by cofilin, Aip1, and coronin.The Journal of biological chemistry · 2020Article
- Directional allosteric regulation of protein filament length.Physical review. E · 2020Article
- Thermal fracture kinetics of heterogeneous semiflexible polymers.Soft matter · 2020Article
- Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments.Proceedings of the National Academy of Sciences of the United States of America · 2020Article
- Plastic Deformation and Fragmentation of Strained Actin Filaments.Biophysical journal · 2019Article
- Torsional stress generated by ADF/cofilin on cross-linked actin filaments boosts their severing.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Multiscale simulation of actin filaments and actin-associated proteins.Biophysical reviews · 2018Review
- Insights into the Cooperative Nature of ATP Hydrolysis in Actin Filaments.Biophysical journal · 2018Article
- Molecular Consequences of the Myopathy-Related D286G Mutation on Actin Function.Frontiers in physiology · 2018Article
- Phosphomimetic S3D cofilin binds but only weakly severs actin filaments.The Journal of biological chemistry · 2017Article
- Actin Filament Strain Promotes Severing and Cofilin Dissociation.Biophysical journal · 2017Article
- Myopathy-inducing mutation H40Y in ACTA1 hampers actin filament structure and function.Biochimica et biophysica acta · 2016Article
- Cations Stiffen Actin Filaments by Adhering a Key Structural Element to Adjacent Subunits.The journal of physical chemistry. B · 2016Article
Corrections and comments
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
The actin regulatory protein cofilin plays a central role in actin assembly dynamics by severing filaments and increasing the concentration of ends from which subunits add and dissociate. Cofilin binding modifies the average structure and mechanical properties of actin filaments, thereby promoting fragmentation of partially decorated filaments at boundaries of bare and cofilin-decorated segments. Despite extensive evidence for cofilin-dependent changes in filament structure and mechanics, it is unclear how the two processes are linked at the molecular level. Here, we use molecular dynamics simulations and coarse-grained analyses to evaluate the molecular origins of the changes in filament compliance due to cofilin binding. Filament subunits with bound cofilin are less flat and maintain a significantly more open nucleotide cleft than bare filament subunits. Decorated filament segments are less twisted, thinner (considering only actin), and less connected than their bare counterparts, which lowers the filament bending persistence length and torsional stiffness. Using coarse-graining as an analysis method reveals that cofilin binding increases the average distance between the adjacent long-axis filament subunit, thereby weakening their interaction. In contrast, a fraction of lateral filament subunit contacts are closer and presumably stronger with cofilin binding. A cofilactin interface contact identified by cryo-electron microscopy is unstable during simulations carried out at 310K, suggesting that this particular interaction may be short lived at ambient temperatures. These results reveal the molecular origins of cofilin-dependent changes in actin filament mechanics that may promote filament severing.
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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.