ArticleProceedings of the National Academy of Sciences of the United States of America2018
Helical rotation of the diaphanous-related formin mDia1 generates actin filaments resistant to cofilin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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31 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
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- Multiple Mechanisms to Regulate Actin Functions: "Fundamental" Versus Lineage-Specific Mechanisms and Hierarchical Relationships.Biomolecules · 2025Review
- Article
- Transmembrane formins as active cargoes of membrane trafficking.Journal of experimental botany · 2024Review
- Cofilin-mediated actin filament network flexibility facilitates 2D to 3D actomyosin shape change.European journal of cell biology · 2024Article
- Disassembly of bundled F-actin and cellular remodeling via an interplay of Mical, cofilin, and F-actin crosslinkers.Proceedings of the National Academy of Sciences of the United States of America · 2023Article
- Article
- MICAL-mediated oxidation of actin and its effects on cytoskeletal and cellular dynamics.Frontiers in cell and developmental biology · 2023Review
- Antagonistic Activities of Fmn2 and ADF Regulate Axonal F-Actin Patch Dynamics and the Initiation of Collateral Branching.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2022Article
- How torque on formins is relaxed strongly affects cellular swirling.Biophysical journal · 2022Article
- Filopodia rotate and coil by actively generating twist in their actin shaft.Nature communications · 2022Article
- Cooperative bundling by fascin generates actin structures with architectures that depend on filament length.Frontiers in cell and developmental biology · 2022Article
- Review
- Septins and a formin have distinct functions in anaphase chiral cortical rotation in theMolecular biology of the cell · 2021Article
- LIM domain proteins in cell mechanobiology.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Articular Chondrocyte Phenotype Regulation through the Cytoskeleton and the Signaling Processes That Originate from or Converge on the Cytoskeleton: Towards a Novel Understanding of the Intersection between Actin Dynamics and Chondrogenic Function.International journal of molecular sciences · 2021Review
- Cytoskeletal Transport, Reorganization, and Fusion Regulation in Mast Cell-Stimulus Secretion Coupling.Frontiers in cell and developmental biology · 2021Review
- Biased localization of actin binding proteins by actin filament conformation.Nature communications · 2020Article
- F-Actin Cytoskeleton Network Self-Organization Through Competition and Cooperation.Annual review of cell and developmental biology · 2020Review
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The complex interplay between actin regulatory proteins facilitates the formation of diverse cellular actin structures. Formin homology proteins (formins) play an essential role in the formation of actin stress fibers and yeast actin cables, to which the major actin depolymerizing factor cofilin barely associates. In vitro, F-actin decorated with cofilin exhibits a marked increase in the filament twist. On the other hand, a mammalian formin mDia1 rotates along the long-pitch actin helix during processive actin elongation (helical rotation). Helical rotation may impose torsional force on F-actin in the opposite direction of the cofilin-induced twisting. Here, we show that helical rotation of mDia1 converts F-actin resistant to cofilin both in vivo and in vitro. F-actin assembled by mDia1 without rotational freedom became more resistant to the severing and binding activities of cofilin than freely rotatable F-actin. Electron micrographic analysis revealed untwisting of the long-pitch helix of F-actin elongating from mDia1 on tethering of both mDia1 and the pointed end side of the filament. In cells, single molecules of mDia1ΔC63, an activated mutant containing N-terminal regulatory domains, showed tethering to cell structures more frequently than autoinhibited wild-type mDia1 and mDia1 devoid of N-terminal domains. Overexpression of mDia1ΔC63 induced the formation of F-actin, which has prolonged lifetime and accelerates dissociation of cofilin. Helical rotation of formins may thus serve as an F-actin stabilizing mechanism by which a barbed end-bound molecule can enhance the stability of a filament over a long range.
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