Evidence map›Paper›PMID 20532239›Full record

ArticlePLoS biology2010

Molecular basis for the dual function of Eps8 on actin dynamics: bundling and capping.

Maud Hertzog, Francesca Milanesi, Larnele Hazelwood, Andrea Disanza, HongJun Liu, Emilie Perlade, Maria Grazia Malabarba, Sebastiano Pasqualato, Alessio Maiolica, Stefano Confalonieri and 9 more

Open access · goldAbstract read
In one paragraph

Article in PLoS biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 68 papers.

0numbers the graph read from it
0cells of the map it votes in
68citing papers in PubMed
4.0field-weighted citation impact, top 6% 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

68 citing papers in PubMed, 101 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Mechanisms of actin disassembly and turnover.The Journal of cell biology · 2023
    Review
  10. Article
  11. Article
  12. Article
  13. Review
  14. Building the brush border, one microvillus at a time.Current opinion in cell biology · 2023
    Review
  15. Article
  16. Targeting of microvillus protein Eps8 by the NleH effector kinases from enteropathogenicProceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  17. Article
  18. Review
  19. Article
  20. Article

8 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

19 authors at 6 institutions in 4 countries.

Maud HertzogIFOM, Fondazione Istituto FIRC di Oncologia Molecolare, Milan, Italy.
Francesca Milanesi
Larnele Hazelwood
Andrea Disanza
HongJun Liu
Emilie Perlade
Maria Grazia Malabarba
Sebastiano Pasqualato
Alessio Maiolica
Stefano Confalonieri
Christophe Le Clainche
Nina Offenhauser
Jennifer Block
Klemens Rottner
Pier Paolo Di Fiore
Marie-France Carlier
Niels Volkmann
Dorit Hanein
Giorgio Scita
FIRC Institute of Molecular Oncology · ITSanford Burnham Prebys Medical Discovery Institute · USEuropean Institute of Oncology · ITHelmholtz Centre for Infection Research · DELaboratoire d'Enzymologie et Biochimie Structurales · FRUniversity of Milan · IT

Funding

STRUCTUREU54GM064346 · NIGMS · UNIVERSITY OF VIRGINIA CHARLOTTESVILLE · PI IMPERIALI, BARBARA · 2001 to 2010
$74.9M
Automated docking and modeling for electron microscopyR01GM076503 · NIGMS · SANFORD BURNHAM PREBYS MEDICAL DISCOVERY INSTITUTE · PI VOLKMANN, NIELS · 2006 to 2010
$1.4M
NIGMS NIH HHS GM076503NIGMS NIH HHS R01 GM076503NIGMS NIH HHS U54 GM064346
6 · The paper itself

Abstract

Actin capping and cross-linking proteins regulate the dynamics and architectures of different cellular protrusions. Eps8 is the founding member of a unique family of capping proteins capable of side-binding and bundling actin filaments. However, the structural basis through which Eps8 exerts these functions remains elusive. Here, we combined biochemical, molecular, and genetic approaches with electron microscopy and image analysis to dissect the molecular mechanism responsible for the distinct activities of Eps8. We propose that bundling activity of Eps8 is mainly mediated by a compact four helix bundle, which is contacting three actin subunits along the filament. The capping activity is mainly mediated by a amphipathic helix that binds within the hydrophobic pocket at the barbed ends of actin blocking further addition of actin monomers. Single-point mutagenesis validated these modes of binding, permitting us to dissect Eps8 capping from bundling activity in vitro. We further showed that the capping and bundling activities of Eps8 can be fully dissected in vivo, demonstrating the physiological relevance of the identified Eps8 structural/functional modules. Eps8 controls actin-based motility through its capping activity, while, as a bundler, is essential for proper intestinal morphogenesis of developing Caenorhabditis elegans.

Indexed as

ActinsAdaptor Proteins, Signal TransducingHumansIntracellular Signaling Peptides and ProteinsMass SpectrometryMicroscopy, ElectronModels, MolecularProtein BindingThermodynamicsActinsAdaptor Proteins, Signal TransducingEPS8 protein, humanIntracellular Signaling Peptides and Proteins

Identifiers

PMID20532239
PMCPMC2879411
OpenAlexW1997447186

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.