Evidence map›Paper›PMID 18625842›Full record

ArticleThe Journal of cell biology2008

Structure of the actin-depolymerizing factor homology domain in complex with actin.

Ville O Paavilainen, Esko Oksanen, Adrian Goldman, Pekka Lappalainen

Abstract read
In one paragraph

Article in The Journal of cell biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 91 papers.

0numbers the graph read from it
0cells of the map it votes in
91citing papers in PubMed
–field-weighted citation impact
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

91 citing papers in PubMed.

  1. Article
  2. Article
  3. Regulation of actin dynamics by Twinfilin.Current opinion in cell biology · 2025
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Structure and activity of a thermally stable mutant of Acanthamoeba actophorin.Acta crystallographica. Section F, Structural biology communications · 2022
    Article
  11. Review
  12. Unravelling the Biology of EhActo as the First Cofilin FromFrontiers in cell and developmental biology · 2022
    Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Role of Cofilin in Alzheimer's Disease.Frontiers in cell and developmental biology · 2020
    Review
  19. Review
  20. Article

31 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

4 authors.

Ville O PaavilainenProgram in Cellular Biotechnology, Institute of Biotechnology, University of Helsinki, Helsinki FIN-00014, Finland.
Esko Oksanen
Adrian Goldman
Pekka Lappalainen

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin dynamics provide the driving force for many cellular processes including motility and endocytosis. Among the central cytoskeletal regulators are actin-depolymerizing factor (ADF)/cofilin, which depolymerizes actin filaments, and twinfilin, which sequesters actin monomers and caps filament barbed ends. Both interact with actin through an ADF homology (ADF-H) domain, which is also found in several other actin-binding proteins. However, in the absence of an atomic structure for the ADF-H domain in complex with actin, the mechanism by which these proteins interact with actin has remained unknown. Here, we present the crystal structure of twinfilin's C-terminal ADF-H domain in complex with an actin monomer. This domain binds between actin subdomains 1 and 3 through an interface that is conserved among ADF-H domain proteins. Based on this structure, we suggest a mechanism by which ADF/cofilin and twinfilin inhibit nucleotide exchange of actin monomers and present a model for how ADF/cofilin induces filament depolymerization by weakening intrafilament interactions.

Indexed as

Sequence Homology, Amino AcidActin CytoskeletonActin Depolymerizing FactorsActinsAdenosine TriphosphateAmino Acid SequenceAnimalsConserved SequenceCrystallography, X-RayDestrinGelsolinMiceMicrofilament ProteinsModels, MolecularMolecular Sequence DataProtein BindingActin Depolymerizing FactorsActinsAdenosine TriphosphateDestrinGelsolinMicrofilament ProteinsTwf1 protein, mouse

Identifiers

PMID18625842
PMCPMC2447895

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Registered trials

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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.