ArticleThe Journal of cell biology2021
Twinfilin bypasses assembly conditions and actin filament aging to drive barbed end depolymerization.
Article in The Journal of cell biology, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 33 papers.
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Who cites it
33 citing papers in PubMed.
- Leiomodin 2 is a processive pointed-end elongator of actin filaments.Nature communications · 2026Article
- Leiomodin 2 functions as a processive pointed-end elongator of actin filaments.bioRxiv : the preprint server for biology · 2026Article
- Twinfilin modulates tissue contractility through uncapping of capping protein in C. elegans.Development (Cambridge, England) · 2025Article
- Structure and Functions of Actin and Actin-Binding Proteins inPathogens (Basel, Switzerland) · 2025Review
- Reconstituted systems for studying the architecture and dynamics of actin networks.The Biochemical journal · 2025Review
- Twinfilin is a nonprocessive depolymerase which synergizes with formin to dramatically accelerate actin filament uncapping by 300-fold.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Two ligands of Arp2/3 complex, yeast coronin and GMF, interact and synergize in pruning branched actin networks.The Journal of biological chemistry · 2025Article
- The actin filament pointed-end depolymerase Srv2/CAP depolymerizes barbed ends, displaces capping protein, and promotes formin processivity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Regulation of actin dynamics by Twinfilin.Current opinion in cell biology · 2025Review
- Structural and functional mechanisms of actin isoforms.The FEBS journal · 2025Review
- Actin filament dynamics at barbed ends: New structures, new insights.Current opinion in cell biology · 2024Review
- Multicomponent depolymerization of actin filament pointed ends by cofilin and cyclase-associated protein depends upon filament age.European journal of cell biology · 2024Article
- Multicomponent depolymerization of actin filament pointed ends by cofilin and cyclase-associated protein depends upon filament age.bioRxiv : the preprint server for biology · 2024Article
- Mechanism of actin capping protein recruitment and turnover during clathrin-mediated endocytosis.The Journal of cell biology · 2024Article
- Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023Review
- Cyclase-associated protein interacts with actin filament barbed ends to promote depolymerization and formin displacement.The Journal of biological chemistry · 2023Article
- The multiple links between actin and mitochondria.Nature reviews. Molecular cell biology · 2023Review
- Multicomponent regulation of actin barbed end assembly by twinfilin, formin and capping protein.Nature communications · 2023Article
- Multicomponent regulation of actin barbed end assembly by twinfilin, formin and capping protein.bioRxiv : the preprint server for biology · 2023Article
- Actin Bundles Dynamics and Architecture.Biomolecules · 2023Review
Corrections and comments
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Authors and funding
4 authors.
Funding
Abstract
Cellular actin networks grow by ATP-actin addition at filament barbed ends and have long been presumed to depolymerize at their pointed ends, primarily after filaments undergo "aging" (ATP hydrolysis and Pi release). The cytosol contains high levels of actin monomers, which favors assembly over disassembly, and barbed ends are enriched in ADP-Pi actin. For these reasons, the potential for a barbed end depolymerization mechanism in cells has received little attention. Here, using microfluidics-assisted TIRF microscopy, we show that mouse twinfilin, a member of the ADF-homology family, induces depolymerization of ADP-Pi barbed ends even under assembly-promoting conditions. Indeed, we observe in single reactions containing micromolar concentrations of actin monomers the simultaneous rapid elongation of formin-bound barbed ends and twinfilin-induced depolymerization of free barbed ends. The data show that twinfilin catalyzes dissociation of subunits from ADP-Pi barbed ends and thereby bypasses filament aging prerequisites to disassemble newly polymerized actin filaments.
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