ArticleThe Journal of biological chemistry2018
Molecular mechanism for inhibition of twinfilin by phosphoinositides.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 10 papers.
What it found
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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.
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Who cites it
10 citing papers in PubMed, 18 citations in OpenAlex.
- 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
- 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 capping protein regulates postsynaptic spine development through CPI-motif interactions.Frontiers in molecular neuroscience · 2022Article
- Twinfilin uncaps filament barbed ends to promote turnover of lamellipodial actin networks.Nature cell biology · 2021Article
- Predicting Genetic Variation Severity Using Machine Learning to Interpret Molecular Simulations.Biophysical journal · 2021Article
- Cytoskeletal Remodeling in Cancer.Biology · 2020Review
- Multiscale Simulations of Biological Membranes: The Challenge To Understand Biological Phenomena in a Living Substance.Chemical reviews · 2019Article
- Computational Modeling of Realistic Cell Membranes.Chemical reviews · 2019Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Membrane phosphoinositides control organization and dynamics of the actin cytoskeleton by regulating the activities of several key actin-binding proteins. Twinfilin is an evolutionarily conserved protein that contributes to cytoskeletal dynamics by interacting with actin monomers, filaments, and the heterodimeric capping protein. Twinfilin also binds phosphoinositides, which inhibit its interactions with actin, but the underlying mechanism has remained unknown. Here, we show that the high-affinity binding site of twinfilin for phosphoinositides is located at the C-terminal tail region, whereas the two actin-depolymerizing factor (ADF)/cofilin-like ADF homology domains of twinfilin bind phosphoinositides only with low affinity. Mutagenesis and biochemical experiments combined with atomistic molecular dynamics simulations reveal that the C-terminal tail of twinfilin interacts with membranes through a multivalent electrostatic interaction with a preference toward phosphatidylinositol 3,5-bisphosphate (PI(3,5)P
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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.