ArticleProceedings of the National Academy of Sciences of the United States of America2007
Structural basis and evolutionary origin of actin filament capping by twinfilin.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 77 citations in OpenAlex.
- 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
- Regulation of actin dynamics by Twinfilin.Current opinion in cell biology · 2025Review
- Cytoskeleton-associated gelsolin responds to the midgut distention process in saline meal-fed Aedes aegypti and affects arbovirus dissemination from the midgut.FASEB journal : official publication of the Federation of American Societies for Experimental 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
- 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
- Human deafness-associated variants alter the dynamics of key molecules in hair cell stereocilia F-actin cores.Human genetics · 2022Review
- Actin capping protein regulates postsynaptic spine development through CPI-motif interactions.Frontiers in molecular neuroscience · 2022Article
- Alteration of twinfilin1 expression underlies opioid withdrawal-induced remodeling of actin cytoskeleton at synapses and formation of aversive memory.Molecular psychiatry · 2021Article
- Deficiency of Klc2 Induces Low-Frequency Sensorineural Hearing Loss in C57BL/6 J Mice and Human.Molecular neurobiology · 2021Article
- Carbonic anhydrase seven bundles filamentous actin and regulates dendritic spine morphology and density.EMBO reports · 2021Article
- Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks.Nature cell biology · 2021Article
- Twinfilin bypasses assembly conditions and actin filament aging to drive barbed end depolymerization.The Journal of cell biology · 2021Article
- The structure of the actin filament uncapping complex mediated by twinfilin.Science advances · 2021Article
- A Pan-Cancer Analysis of the Oncogenic Role of Twinfilin Actin Binding Protein 1 in Human Tumors.Frontiers in oncology · 2021Article
- AimB Is a Small Protein Regulator of Cell Size and MreB Assembly.Biophysical journal · 2020Article
- CAPt'n of Actin Dynamics: Recent Advances in the Molecular, Developmental and Physiological Functions of Cyclase-Associated Protein (CAP).Frontiers in cell and developmental biology · 2020Review
- MCTS1 Directly Binds to TWF1 and Synergistically Modulate Cyclin D1 and C-Myc Translation in Luminal A/B Breast Cancer Cells.OncoTargets and therapy · 2020Article
- MicroRNA-486-5p improves nonsmall-cell lung cancer chemotherapy sensitivity and inhibits epithelial-mesenchymal transition by targeting twinfilin actin binding protein 1.The Journal of international medical research · 2019Article
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Authors and funding
8 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Dynamic reorganization of the actin cytoskeleton is essential for motile and morphological processes in all eukaryotic cells. One highly conserved protein that regulates actin dynamics is twinfilin, which both sequesters actin monomers and caps actin filament barbed ends. Twinfilin is composed of two ADF/cofilin-like domains, Twf-N and Twf-C. Here, we reveal by systematic domain-swapping/inactivation analysis that the two functional ADF-H domains of twinfilin are required for barbed-end capping and that Twf-C plays a critical role in this process. However, these domains are not functionally equivalent. NMR-structure and mutagenesis analyses, together with biochemical and motility assays showed that Twf-C, in addition to its binding to G-actin, interacts with the sides of actin filaments like ADF/cofilins, whereas Twf-N binds only G-actin. Our results indicate that during filament barbed-end capping, Twf-N interacts with the terminal actin subunit, whereas Twf-C binds between two adjacent subunits at the side of the filament. Thus, the domain requirement for actin filament capping by twinfilin is remarkably similar to that of gelsolin family proteins, suggesting the existence of a general barbed-end capping mechanism. Furthermore, we demonstrate that a synthetic protein consisting of duplicated ADF/cofilin domains caps actin filament barbed ends, providing evidence that the barbed-end capping activity of twinfilin arose through a duplication of an ancient ADF/cofilin-like domain.
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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.