ArticleThe Journal of biological chemistry2006
Binding of myotrophin/V-1 to actin-capping protein: implications for how capping protein binds to the filament barbed end.
Article in The Journal of biological chemistry, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 45 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
45 citing papers in PubMed.
- Mechanisms of CARMIL dimerization, autoinhibition, and capping protein binding.Science advances · 2026Article
- Identification of a novel real-time PCR reference gene panel for EA.hy926 endothelial cells in different growth States and with DHA treatment.Scientific reports · 2026Article
- Coordinated regulation of Capping Protein by CARMIL and V-1/myotrophin.The Journal of biological chemistry · 2026Review
- Cardiac CapZ Regulation During Acute Exercise in Female Mice.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 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
- Reconstitution of Arp2/3-nucleated actin assembly with proteins CP, V-1, and CARMIL.Current biology : CB · 2024Article
- Reconstitution of Arp2/3-Nucleated Actin Assembly with CP, V-1 and CARMIL.bioRxiv : the preprint server for biology · 2024Article
- Bsp1, a fungal CPI motif protein, regulates actin filament capping in endocytosis and cytokinesis.Molecular biology of the cell · 2024Article
- MicroRNA-1 Deficiency Is a Primary Etiological Factor Disrupting Cardiac Contractility and Electrophysiological Homeostasis.Circulation. Arrhythmia and electrophysiology · 2024Article
- Mechanism of actin capping protein recruitment and turnover during clathrin-mediated endocytosis.The Journal of cell biology · 2024Article
- Biophysical Mechanism of Allosteric Regulation of Actin Capping Protein.Journal of molecular biology · 2023Article
- Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023Review
- Evolutionary tuning of barbed end competition allows simultaneous construction of architecturally distinct actin structures.The Journal of cell biology · 2023Article
- Article
- Dual regulation of the actin cytoskeleton by CARMIL-GAP.Journal of cell science · 2022Article
- Actin capping protein regulates postsynaptic spine development through CPI-motif interactions.Frontiers in molecular neuroscience · 2022Article
- Repression ofScience advances · 2021Article
- Review
- MicroRNA-mediated regulation of glucose and lipid metabolism.Nature reviews. Molecular cell biology · 2021Review
- Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks.Nature cell biology · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
4 authors.
Funding
Abstract
The heterodimeric actin-capping protein (CP) regulates actin assembly and cell motility by binding tightly to the barbed end of the actin filament. Here we demonstrate that myotrophin/V-1 binds directly to CP in a 1:1 molar ratio with a Kd of 10-50 nm. V-1 binding inhibited the ability of CP to cap the barbed ends of actin filaments. The actin-binding COOH-terminal region, the "tentacle," of the CP beta subunit was important for binding V-1, with lesser contributions from the alpha subunit COOH-terminal region and the body of the protein. V-1 appears to be unable to bind to CP that is on the barbed end, based on the observations that V-1 had no activity in an uncapping assay and that the V-1.CP complex had no capping activity. Two loops of V-1, which extend out from the alpha-helical backbone of this ankyrin repeat protein, were necessary for V-1 to bind CP. Parallel computational studies determined a bound conformation of the beta tentacle with V-1 that is consistent with these findings, and they offered insight into experimentally observed differences between the alpha1 and alpha2 isoforms as well as the mutant lacking the alpha tentacle. These results support and extend our "wobble" model for CP binding to the actin filament, in which the two COOH-terminal regions of CP bind independently to the actin filament, and bound CP is able to wobble when attached only via its mobile beta-subunit tentacle. This model is also supported by molecular dynamics simulations of CP reported here. The existence of the wobble state may be important for actin dynamics in cells.
Indexed as
Identifiers
What OpenQuestion holds
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.