ReviewCurrent opinion in cell biology2025
Regulation of actin dynamics by Twinfilin.
Review in Current opinion in cell biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 5 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
5 citing papers in PubMed.
- Coordinated regulation of Capping Protein by CARMIL and V-1/myotrophin.The Journal of biological chemistry · 2026Review
- Twinfilin modulates tissue contractility through uncapping of capping protein in C. elegans.Development (Cambridge, England) · 2025Article
- Epigenetic Mechanisms Shaping Spine Regulation: Unveiling the Role of Cytoskeletal Dynamics and Localized Protein Synthesis.Molecular neurobiology · 2025Review
- 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
- The actin filament pointed-end depolymerase Srv2/CAP depolymerizes barbed ends, displaces capping protein, and promotes formin processivity.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
2 authors.
Funding
Abstract
Twinfilin is an evolutionarily conserved actin-binding protein initially mischaracterized as a tyrosine kinase but later recognized as a key regulator of cellular actin dynamics. As a member of the ADF-H family, twinfilin binds both actin monomers and filaments. Its role in sequestering G-actin is well-established, but its effects on actin filaments have been debated. While early studies suggested twinfilin caps filament barbed ends, later research demonstrated its role in nucleotide-specific barbed-end depolymerization. Further, it was initially thought to be a processive depolymerase. Recent structural and single-molecule studies have however challenged this view, indicating that twinfilin binding events result in the removal of only one or two actin subunits from the barbed end. Additionally, twinfilin directly binds capping protein (CP) and facilitates uncapping of CP-bound barbed ends. Here, we summarize twinfilin's cellular and tissue-specific localization, and examine its evolving role in regulating cellular actin dynamics in light of its known biochemical functions.
Indexed as
Identifiers
What Socratic 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 Socratic graph.