Evidence map›Paper›PMID 25706231›Full record

ArticleeLife2015

Side-binding proteins modulate actin filament dynamics.

Alvaro H Crevenna, Marcelino Arciniega, Aurélie Dupont, Naoko Mizuno, Kaja Kowalska, Oliver F Lange, Roland Wedlich-Söldner, Don C Lamb

Abstract read
In one paragraph

Article in eLife, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 papers.

0numbers the graph read from it
0cells of the map it votes in
17citing 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

17 citing papers in PubMed.

  1. ATP-dependent actin barbed-end fluctuations at steady state.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  2. Article
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  4. Turn-On Protein Switches for Controlling Actin Binding in Cells.bioRxiv : the preprint server for biology · 2023
    Article
  5. Article
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  7. Article
  8. Article
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  10. Myosin 1b is an actin depolymerase.Nature communications · 2019
    Article
  11. Article
  12. Article
  13. Article
  14. Discovery of functional interactions among actin regulators by analysis of image fluctuations in an unperturbed motile cell system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2018
    Review
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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

8 authors.

Alvaro H CrevennaPhysical Chemistry, Department of Chemistry and Center for Nanoscience, Ludwig-Maximilians-Universität München, Munich, Germany.ORCID http://orcid.org/0000-0002-5580-3711
Marcelino ArciniegaMax Planck Institute of Biochemistry, Martinsried, Germany.
Aurélie DupontPhysical Chemistry, Department of Chemistry and Center for Nanoscience, Ludwig-Maximilians-Universität München, Munich, Germany.
Naoko MizunoCellular and Membrane Trafficking, Max Planck Institute of Biochemistry, Martinsried, Germany.
Kaja KowalskaCellular Dynamics and Cell Patterning, Max Planck Institute of Biochemistry, Martinsried, Germany.
Oliver F LangeDepartment of Chemistry, Technische Universität München, Garching, Germany.
Roland Wedlich-SöldnerCellular Dynamics and Cell Patterning, Max Planck Institute of Biochemistry, Martinsried, Germany.
Don C LambPhysical Chemistry, Department of Chemistry and Center for Nanoscience, Ludwig-Maximilians-Universität München, Munich, Germany.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Actin filament dynamics govern many key physiological processes from cell motility to tissue morphogenesis. A central feature of actin dynamics is the capacity of filaments to polymerize and depolymerize at their ends in response to cellular conditions. It is currently thought that filament kinetics can be described by a single rate constant for each end. In this study, using direct visualization of single actin filament elongation, we show that actin polymerization kinetics at both filament ends are strongly influenced by the binding of proteins to the lateral filament surface. We also show that the pointed-end has a non-elongating state that dominates the observed filament kinetic asymmetry. Estimates of flexibility as well as effects on fragmentation and growth suggest that the observed kinetic diversity arises from structural alteration. Tuning elongation kinetics by exploiting the malleability of the filament structure may be a ubiquitous mechanism to generate a rich variety of cellular actin dynamics.

Indexed as

PolymerizationActin CytoskeletonActininActinsAdenosine TriphosphateAlgorithmsAnimalsCarrier ProteinsCell Adhesion MoleculesChickensFilaminsKineticsMicrofilament ProteinsMicroscopy, ElectronMicroscopy, FluorescenceModels, BiologicalActininActinsAdenosine TriphosphateCarrier ProteinsCell Adhesion MoleculesFilaminsMicrofilament ProteinsMyosinsPhosphoproteinsactinactin-binding proteinsbiophysicscell biologystructural biologyTIRFtreadmilling

Identifiers

PMID25706231
PMCPMC4375888

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.