ArticleThe Journal of cell biology2001
Interactions with PIP2, ADP-actin monomers, and capping protein regulate the activity and localization of yeast twinfilin.
Article in The Journal of cell biology, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.
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Who cites it
91 citing papers in PubMed, 180 citations in OpenAlex.
- Twinfilin modulates tissue contractility through uncapping of capping protein in C. elegans.Development (Cambridge, England) · 2025Article
- A Microfluidic Platform for Actin-Based Membrane Remodeling Reveals the Stabilizing Role of Branched Actin Networks on Lipid Microdomains.Small science · 2025Article
- 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
- Phosphoinositide signaling at the cytoskeleton in the regulation of cell dynamics.Cell death & disease · 2025Review
- Regulation of actin dynamics by Twinfilin.Current opinion in cell biology · 2025Review
- Bsp1, a fungal CPI motif protein, regulates actin filament capping in endocytosis and cytokinesis.Molecular biology of the cell · 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
- Multicomponent regulation of actin barbed end assembly by twinfilin, formin and capping protein.Nature communications · 2023Article
- Cross-Platform Synaptic Network Analysis of Human Entorhinal Cortex Identifies TWF2 as a Modulator of Dendritic Spine Length.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2023Article
- Recycling of the actin monomer pool limits the lifetime of network turnover.The EMBO journal · 2023Article
- Multicomponent regulation of actin barbed end assembly by twinfilin, formin and capping protein.bioRxiv : the preprint server for biology · 2023Article
- Mechanism of actin filament branch formation by Arp2/3 complex revealed by a high-resolution cryo-EM structureof the branch junction.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Structural basis of rapid actin dynamics in the evolutionarily divergent Leishmania parasite.Nature communications · 2022Article
- Unconcerted conformational changes in Arp2/3 complex integrate multiple activating signals to assemble functional actin networks.Current biology : CB · 2022Article
- Actin capping protein regulates postsynaptic spine development through CPI-motif interactions.Frontiers in molecular neuroscience · 2022Article
- Oncogenic role of TWF2 in human tumors: A pan-cancer analysis.Open medicine (Warsaw, Poland) · 2022Article
- Deficiency of Klc2 Induces Low-Frequency Sensorineural Hearing Loss in C57BL/6 J Mice and Human.Molecular neurobiology · 2021Article
- The dynein light chain protein Tda2 functions as a dimerization engine to regulate actin capping protein during endocytosis.Molecular biology of the cell · 2021Article
- Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks.Nature cell biology · 2021Article
31 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
Twinfilin is a ubiquitous actin monomer-binding protein that regulates actin filament turnover in yeast and mammalian cells. To elucidate the mechanism by which twinfilin contributes to actin filament dynamics, we carried out an analysis of yeast twinfilin, and we show here that twinfilin is an abundant protein that localizes to cortical actin patches in wild-type yeast cells. Native gel assays demonstrate that twinfilin binds ADP-actin monomers with higher affinity than ATP-actin monomers. A mutant twinfilin that does not interact with actin monomers in vitro no longer localizes to cortical actin patches when expressed in yeast, suggesting that the ability to interact with actin monomers may be essential for the localization of twinfilin. The localization of twinfilin to the cortical actin cytoskeleton is also disrupted in yeast strains where either the CAP1 or CAP2 gene, encoding for the alpha and beta subunits of capping protein, is deleted. Purified twinfilin and capping protein form a complex on native gels. Twinfilin also interacts with phosphatidylinositol 4,5-bisphosphate (PI[4,5]P2), and its actin monomer-sequestering activity is inhibited by PI(4,5)P2. Based on these results, we propose a model for the biological role of twinfilin as a protein that localizes actin monomers to the sites of rapid filament assembly in cells.
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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.