ArticleProceedings of the National Academy of Sciences of the United States of America2020
Structures of cofilin-induced structural changes reveal local and asymmetric perturbations of actin filaments.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 58 papers.
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Who cites it
58 citing papers in PubMed, 54 citations in OpenAlex.
- Synergistic assembly, disassembly, and protection of complex forms of bundled F-actin.The Journal of cell biology · 2026Article
- Structural mechanisms of drebrin-mediated F-actin network modulation.Nature communications · 2026Article
- Mechanisms of actin-binding proteins in glycolysis-cytoskeleton coupling.Journal of translational medicine · 2026Review
- Bound for the nucleus: defining the molecular principles of cargo selection by importin 9.bioRxiv : the preprint server for biology · 2026Article
- Mechanisms of disassembly at the actin filament pointed and barbed ends.Science advances · 2026Article
- Molecular architecture of Influenza A virions.bioRxiv : the preprint server for biology · 2026Article
- The Baraitser-Winter Cerebrofrontofacial Syndrome Recurrent R196H Variant in Cytoplasmic β-Actin Impairs Its Cellular Polymerization and Stability.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026Article
- The structure of an actin nucleus stabilized by villin.Science advances · 2025Article
- A revised model of nuclear actin import: Importin 9 competes with cofilin, profilin, and RanGTP for actin binding.bioRxiv : the preprint server for biology · 2025Article
- Optogenetic actin network assembly on lipid bilayer uncovers the network density-dependent functions of actin-binding proteins.Nature communications · 2025Article
- Hydrolysis-dependent severing tunes internal monomeric heterogeneity to shape actin length distributions.bioRxiv : the preprint server for biology · 2025Article
- Fungal-derived methyldeoxaphomins targetProceedings of the National Academy of Sciences of the United States of America · 2025Article
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Mechanism of actin filament severing and capping by gelsolin.Nature structural & molecular biology · 2025Article
- Regulation and signaling of the LIM domain kinases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025Review
- Electrical Forces Improve Memory in Old Age.Reviews of physiology, biochemistry and pharmacology · 2025Review
- Cracked actin filaments as mechanosensitive receptors.Biophysical journal · 2024Article
- Article
- Molecular simulation approaches to probing the effects of mechanical forces in the actin cytoskeleton.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Turn-on protein switches for controlling actin binding in cells.Nature communications · 2024Article
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6 authors at 1 institution in 1 country.
Funding
Abstract
Members of the cofilin/ADF family of proteins sever actin filaments, increasing the number of filament ends available for polymerization or depolymerization. Cofilin binds actin filaments with positive cooperativity, forming clusters of contiguously bound cofilin along the filament lattice. Filament severing occurs preferentially at boundaries between bare and cofilin-decorated (cofilactin) segments and is biased at 1 side of a cluster. A molecular understanding of cooperative binding and filament severing has been impeded by a lack of structural data describing boundaries. Here, we apply methods for analyzing filament cryo-electron microscopy (cryo-EM) data at the single subunit level to directly investigate the structure of boundaries within partially decorated cofilactin filaments. Subnanometer resolution maps of isolated, bound cofilin molecules and an actin-cofilactin boundary indicate that cofilin-induced actin conformational changes are local and limited to subunits directly contacting bound cofilin. An isolated, bound cofilin compromises longitudinal filament contacts of 1 protofilament, consistent with a single cofilin having filament-severing activity. An individual, bound phosphomimetic (S3D) cofilin with weak severing activity adopts a unique binding mode that does not perturb actin structure. Cofilin clusters disrupt both protofilaments, consistent with a higher severing activity at boundaries compared to single cofilin. Comparison of these structures indicates that this disruption is substantially greater at pointed end sides of cofilactin clusters than at the barbed end. These structures, with the distribution of bound cofilin clusters, suggest that maximum binding cooperativity is achieved when 2 cofilins occupy adjacent sites. These results reveal the structural origins of cooperative cofilin binding and actin filament severing.
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