ArticleNature structural & molecular biology2013
Dimeric WH2 domains in Vibrio VopF promote actin filament barbed-end uncapping and assisted elongation.
Article in Nature structural & molecular biology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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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.
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Who cites it
31 citing papers in PubMed, 50 citations in OpenAlex.
- Renaissance at the actin filament pointed end: Mechanisms of assembly, capping and depolymerization.Current opinion in cell biology · 2026Review
- 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
- Antagonistic Effects of Actin-Specific Toxins onBiomolecules · 2024Article
- Disulfidptosis: a novel cell death modality induced by actin cytoskeleton collapse and a promising target for cancer therapeutics.Cell communication and signaling : CCS · 2024Review
- Actin filament dynamics at barbed ends: New structures, new insights.Current opinion in cell biology · 2024Review
- Antagonistic effects of actin-specific toxins onbioRxiv : the preprint server for biology · 2024Article
- Pointed-end processive elongation of actin filaments byScience advances · 2022Article
- Functional Mimicry of Eukaryotic Actin Assembly by Pathogen Effector Proteins.International journal of molecular sciences · 2022Review
- Spire stimulates nucleation by Cappuccino and binds both ends of actin filaments.Molecular biology of the cell · 2020Article
- Compressive three-dimensional super-resolution microscopy with speckle-saturated fluorescence excitation.Nature communications · 2019Article
- Vibrio variations on a type three theme.Current opinion in microbiology · 2019Review
- T3SS effector VopL inhibits the host ROS response, promoting the intracellular survival of Vibrio parahaemolyticus.PLoS pathogens · 2017Article
- Global treadmilling coordinates actin turnover and controls the size of actin networks.Nature reviews. Molecular cell biology · 2017Review
- The bacterial virulence factors VopL and VopF nucleate actin from the pointed end.The Journal of cell biology · 2017Article
- Actin filament assembly by bacterial factors VopL/F: Which end is up?The Journal of cell biology · 2017Article
- Actin-based motility of bacterial pathogens: mechanistic diversity and its impact on virulence.Pathogens and disease · 2016Article
- The WH2 Domain and Actin Nucleation: Necessary but Insufficient.Trends in biochemical sciences · 2016Review
- Role of the C-terminal Extension of Formin 2 in Its Activation by Spire Protein and Processive Assembly of Actin Filaments.The Journal of biological chemistry · 2016Article
- Profilin Interaction with Actin Filament Barbed End Controls Dynamic Instability, Capping, Branching, and Motility.Developmental cell · 2016Article
- Biochemical Activities of the Wiskott-Aldrich Syndrome Homology Region 2 Domains of Sarcomere Length Short (SALS) Protein.The Journal of biological chemistry · 2016Article
Corrections and comments
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Authors and funding
7 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins containing repeats of the WASP homology 2 (WH2) actin-binding module are multifunctional regulators of actin nucleation and assembly. The bacterial effector VopF in Vibrio cholerae, like VopL in Vibrio parahaemolyticus, is a unique homodimer of three WH2 motifs linked by a C-terminal dimerization domain. We show that only the first and third WH2 domains of VopF bind G-actin in a non-nucleating, sequestered conformation. Moreover, dimeric WH2 domains in VopF give rise to unprecedented regulation of actin assembly. Specifically, two WH2 domains on opposite protomers of VopF direct filament assembly from actin or profilin-actin by binding terminal subunits and uncapping capping protein from barbed ends by a new mechanism. Thus, VopF does not nucleate filaments by capping a pointed-end F-actin hexamer. These properties may contribute to VopF pathogenicity, and they show how dimeric WH2 peptides may mediate processive filament growth.
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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.