ArticleThe Journal of biological chemistry2010
Direct observation of the uncapping of capping protein-capped actin filaments by CARMIL homology domain 3.
Article in The Journal of biological chemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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Who cites it
47 citing papers in PubMed, 57 citations in OpenAlex.
- CARMIL membrane-binding domain regulates capping protein and actin assembly.The Journal of biological chemistry · 2026Article
- Mechanisms of CARMIL dimerization, autoinhibition, and capping protein binding.Science advances · 2026Article
- Coordinated regulation of Capping Protein by CARMIL and V-1/myotrophin.The Journal of biological chemistry · 2026Review
- 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
- Reconstitution of Arp2/3-nucleated actin assembly with proteins CP, V-1, and CARMIL.Current biology : CB · 2024Article
- Actin filament dynamics at barbed ends: New structures, new insights.Current opinion in cell biology · 2024Review
- Reconstitution of Arp2/3-Nucleated Actin Assembly with CP, V-1 and CARMIL.bioRxiv : the preprint server for 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
- Dual regulation of the actin cytoskeleton by CARMIL-GAP.Journal of cell science · 2022Article
- Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks.Nature cell biology · 2021Article
- Myosin 18Aα targets the guanine nucleotide exchange factor β-Pix to the dendritic spines of cerebellar Purkinje neurons and promotes spine maturation.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- Crystal structure of human V-1 in the apo form.Acta crystallographica. Section F, Structural biology communications · 2021Article
- The Leucine-Rich Repeat Region of CARMIL1 Regulates IL-1-Mediated ERK Activation, MMP Expression, and Collagen Degradation.Cell reports · 2020Article
- D-Loop Mutation G42A/G46A Decreases Actin Dynamics.Biomolecules · 2020Article
- Allosteric Coupling of CARMIL and V-1 Binding to Capping Protein Revealed by Hydrogen-Deuterium Exchange.Cell reports · 2018Article
- CARMIL family proteins as multidomain regulators of actin-based motility.Molecular biology of the cell · 2017Article
- Model of turnover kinetics in the lamellipodium: implications of slow- and fast- diffusing capping protein and Arp2/3 complex.Physical biology · 2016Article
- Internetwork competition for monomers governs actin cytoskeleton organization.Nature reviews. Molecular cell biology · 2016Article
Corrections and comments
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
Bulk solution assays have shown that the isolated CARMIL homology 3 (CAH3) domain from mouse and Acanthamoeba CARMIL rapidly and potently restores actin polymerization when added to actin filaments previously capped with capping protein (CP). To demonstrate this putative uncapping activity directly, we used total internal reflection microscopy to observe single, CP-capped actin filaments before and after the addition of the CAH3 domain from mouse CARMIL-1 (mCAH3). The addition of mCAH3 rapidly restored the polymerization of individual capped filaments, consistent with uncapping. To verify uncapping, filaments were capped with recombinant mouse CP tagged with monomeric green fluorescent protein (mGFP-CP). Restoration of polymerization upon the addition of mCAH3 was immediately preceded by the complete dissociation of mGFP-CP from the filament end, confirming the CAH3-driven uncapping mechanism. Quantitative analyses showed that the percentage of capped filaments that uncapped increased as the concentration of mCAH3 was increased, reaching a maximum of approximately 90% at approximately 250 nm mCAH3. Moreover, the time interval between mCAH3 addition and uncapping decreased as the concentration of mCAH3 increased, with the half-time of CP at the barbed end decreasing from approximately 30 min without mCAH3 to approximately 10 s with a saturating amount of mCAH3. Finally, using mCAH3 tagged with mGFP, we obtained direct evidence that the complex of CP and mCAH3 has a small but measurable affinity for the barbed end, as inferred from previous studies and kinetic modeling. We conclude that the isolated CAH3 domain of CARMIL (and presumably the intact molecule as well) possesses the ability to uncap CP-capped actin filaments.
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Registered trials
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.