Evidence map›Paper›PMID 16675552›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2006

The bundling activity of vasodilator-stimulated phosphoprotein is required for filopodium formation.

Antje Schirenbeck, Rajesh Arasada, Till Bretschneider, Theresia E B Stradal, Michael Schleicher, Jan Faix

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.

0numbers the graph read from it
0cells of the map it votes in
78citing papers in PubMed
7.5field-weighted citation impact, top 2% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

78 citing papers in PubMed, 158 citations in OpenAlex.

  1. Ovarian germline stem cell dedifferentiation is cytoneme dependent.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
  3. Liquid-like condensates mediate competition between actin branching and bundling.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  4. Review
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  15. What Defines the "Kingdom" Fungi?Microbiology spectrum · 2017
    Review
  16. Article
  17. Ena/VASP proteins regulate activated T-cell trafficking by promoting diapedesis during transendothelial migration.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  18. Article
  19. Review
  20. Article

18 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

6 authors at 4 institutions in 1 country.

Antje SchirenbeckDepartment of Cell Biology, Ludwig Maximilians University, 80336 München, Germany.
Rajesh Arasada
Till Bretschneider
Theresia E B Stradal
Michael Schleicher
Jan Faix
Ludwig-Maximilians-Universität München · DEHelmholtz Centre for Infection Research · DEMax Planck Institute of Biochemistry · DEMedizinische Hochschule Hannover · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Filopodia are highly dynamic finger-like cell protrusions filled with parallel bundles of actin filaments. Previously we have shown that Diaphanous-related formin dDia2 is involved in the formation of filopodia. Another key player for the formation of filopodia across many species is vasodilator-stimulated phosphoprotein (VASP). It has been proposed that the essential role of VASP for formation of filopodia is its competition with capping proteins for filament barbed-end interaction. To better understand the function of VASP in filopodium formation, we analyzed the in vitro and in vivo properties of Dictyostelium VASP (DdVASP) and extended our findings to human VASP. Recombinant VASP from both species nucleated and bundled actin filaments, but did not compete with capping proteins or block depolymerization from barbed ends. Together with the finding that DdVASP binds to the FH2 domain of dDia2, these data indicate that the crucial role of VASP in filopodium formation is different from uncapping of actin filaments. To identify the activity of DdVASP required in this process, rescue experiments of DdVASP-null cells with mutant DdVASP constructs were performed. Only WT DdVASP, but not a mutant lacking the F-actin bundling activity, could rescue the ability of these cells to form WT-like filopodia. Our data suggest that DdVASP is complexed with dDia2 in filopodial tips and support formin-mediated filament elongation by bundling nascent actin filaments.

Indexed as

ActinsAmino Acid SequenceAnimalsCell Adhesion MoleculesDictyosteliumHumansMicrofilament ProteinsMolecular Sequence DataPhosphoproteinsProtozoan ProteinsPseudopodiaRecombinant ProteinsSequence AlignmentTwo-Hybrid System TechniquesVasodilator-Stimulated PhosphoproteinActinsCell Adhesion MoleculesDia2 protein, DictyosteliumMicrofilament ProteinsPhosphoproteinsProtozoan ProteinsRecombinant ProteinsVasodilator-Stimulated Phosphoprotein

Identifiers

PMID16675552
PMCPMC1457090
OpenAlexW2069199145

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.