ArticleScientific reports2016
Cofilin-induced cooperative conformational changes of actin subunits revealed using cofilin-actin fusion protein.
Article in Scientific reports, 2016. 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, 20 citations in OpenAlex.
- Chemotactic motion of coronin-null cells with impaired actin turnover.BMC molecular and cell biology · 2026Article
- Role of N-glycosylation as a determinant of ATG9A conformations and activity.Protein science : a publication of the Protein Society · 2026Article
- Role of Tpm Isoforms Produced by theBiomolecules · 2025Article
- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Biased localization of actin binding proteins by actin filament conformation.Nature communications · 2020Article
- Long-Range and Directional Allostery of Actin Filaments Plays Important Roles in Various Cellular Activities.International journal of molecular sciences · 2020Review
- An Alternative Pin1 Binding and Isomerization Site in the N-Terminus Domain of PSD-95.Frontiers in molecular neuroscience · 2020Article
- Plastic Deformation and Fragmentation of Strained Actin Filaments.Biophysical journal · 2019Article
- K336I mutant actin alters the structure of neighbouring protomers in filaments and reduces affinity for actin-binding proteins.Scientific reports · 2019Article
- Kinesin-binding-triggered conformation switching of microtubules contributes to polarized transport.The Journal of cell biology · 2018Article
- Transient stretch induces cytoskeletal fluidization through the severing action of cofilin.American journal of physiology. Lung cellular and molecular physiology · 2018Article
- Cardiac leiomodin2 binds to the sides of actin filaments and regulates the ATPase activity of myosin.PloS one · 2017Article
- Allosteric regulation by cooperative conformational changes of actin filaments drives mutually exclusive binding with cofilin and myosin.Scientific reports · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To investigate cooperative conformational changes of actin filaments induced by cofilin binding, we engineered a fusion protein made of Dictyostelium cofilin and actin. The filaments of the fusion protein were functionally similar to actin filaments bound with cofilin in that they did not bind rhodamine-phalloidin, had quenched fluorescence of pyrene attached to Cys374 and showed enhanced susceptibility of the DNase loop to cleavage by subtilisin. Quantitative analyses of copolymers made of different ratios of the fusion protein and control actin further demonstrated that the fusion protein affects the structure of multiple neighboring actin subunits in copolymers. Based on these and other recent related studies, we propose a mechanism by which conformational changes induced by cofilin binding is propagated unidirectionally to the pointed ends of the filaments, and cofilin clusters grow unidirectionally to the pointed ends following this path. Interestingly, the fusion protein was unable to copolymerize with control actin at pH 6.5 and low ionic strength, suggesting that the structural difference between the actin moiety in the fusion protein and control actin is pH-sensitive.
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