ArticleBiochemical and biophysical research communications2013
Competitive displacement of cofilin can promote actin filament severing.
Article in Biochemical and biophysical research communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.
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Who cites it
35 citing papers in PubMed, 47 citations in OpenAlex.
- Renaissance at the actin filament pointed end: Mechanisms of assembly, capping and depolymerization.Current opinion in cell biology · 2026Review
- F-actin architecture determines the conversion of chemical energy into mechanical work.Nature communications · 2024Article
- Cofilin-mediated actin filament network flexibility facilitates 2D to 3D actomyosin shape change.European journal of cell biology · 2024Article
- Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023Review
- Cooperative ligand binding to a double-stranded Ising lattice-Application to cofilin binding to actin filaments.PNAS nexus · 2023Article
- Pyramidal neuron morphogenesis requires a septin network that stabilizes filopodia and suppresses lamellipodia during neurite initiation.Current biology : CB · 2023Article
- Coro1B and Coro1C regulate lamellipodia dynamics and cell motility by tuning branched actin turnover.The Journal of cell biology · 2022Article
- Cofilactin filaments regulate filopodial structure and dynamics in neuronal growth cones.Nature communications · 2022Article
- Article
- Catastrophic actin filament bursting by cofilin, Aip1, and coronin.The Journal of biological chemistry · 2020Article
- Synergy between Cyclase-associated protein and Cofilin accelerates actin filament depolymerization by two orders of magnitude.Nature communications · 2019Article
- Coronin 1A depletion restores the nuclear stability and viability of Aip1/Wdr1-deficient neutrophils.The Journal of cell biology · 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
- Real-Time Single-Molecule Kinetic Analyses of AIP1-Enhanced Actin Filament Severing in the Presence of Cofilin.Journal of molecular biology · 2019Article
- Quantitative Variations with pH of Actin Depolymerizing Factor/Cofilin's Multiple Actions on Actin Filaments.Biochemistry · 2019Article
- Functions of actin-interacting protein 1 (AIP1)/WD repeat protein 1 (WDR1) in actin filament dynamics and cytoskeletal regulation.Biochemical and biophysical research communications · 2018Review
- The actin filament bundling protein α-actinin-4 actually suppresses actin stress fibers by permitting actin turnover.The Journal of biological chemistry · 2018Article
- The actin filament twist changes abruptly at boundaries between bare and cofilin-decorated segments.The Journal of biological chemistry · 2018Article
- Phosphomimetic S3D cofilin binds but only weakly severs actin filaments.The Journal of biological chemistry · 2017Article
- Diversity of actin architecture in human osteoclasts: network of curved and branched actin supporting cell shape and intercellular micrometer-level tubes.Molecular and cellular biochemistry · 2017Article
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Cofilin is an essential actin filament severing protein that functions in the dynamic remodeling of the actin cytoskeleton. Filament severing activity is most efficient at sub-stoichiometric cofilin binding densities (i.e. <1 cofilin per actin filament subunit), and peaks when the number density of boundaries (i.e. junctions) between bare and cofilin-decorated segments is maximal. A model in which local topological and mechanical discontinuities lead to preferential fragmentation at boundaries accounts for available experimental data, including direct visualization of cofilin and actin during real-time severing events. The boundary-severing model predicts that ligands (e.g. other actin-binding proteins) that compete with cofilin for actin filament binding and modulate cofilin occupancy on filaments will alter the bare-decorated segment boundary density, and thus, the filament severing activity of cofilin. Here, we directly test this model prediction by evaluating the effects of phalloidin and myosin, two ligands that compete with cofilin for filament binding, on the actin filament binding and severing activities of cofilin. Our experiments demonstrate that competitive displacement of cofilin lowers cofilin occupancy and promotes severing when initial cofilin occupancy is high (i.e. >50%). Even in the presence of competitive ligands, maximum severing activity occurs when cofilin-decorated boundary density is highest, consistent with preferential fragmentation at boundaries. We propose a general "severodyne" framework for the modulation of cofilin-mediated actin filament severing by small molecule or actin-binding protein ligands that compete with cofilin for actin filament binding.
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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.