Evidence map›Paper›PMID 16963509›Full record

ArticleBiophysical journal2006

Actin polymerization serves as a membrane domain switch in model lipid bilayers.

Allen P Liu, Daniel A Fletcher

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 116 papers.

0numbers the graph read from it
0cells of the map it votes in
116citing papers in PubMed
5.8field-weighted citation impact, top 3% 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

116 citing papers in PubMed, 237 citations in OpenAlex.

  1. Article
  2. PIPProceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  3. Polyphenols fromMembranes · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Review
  11. Polysaccharide functionalization reduces lipid vesicle stiffness.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  12. Article
  13. Sorting of complex sphingolipids within the cellular endomembrane systems.Frontiers in cell and developmental biology · 2024
    Review
  14. Review
  15. Article
  16. Article
  17. Self-organizing actin networks drive sequential endocytic protein recruitment and vesicle release on synthetic lipid bilayers.Proceedings of the National Academy of Sciences of the United States of America · 2023
    Article
  18. Article
  19. Article
  20. Article

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

4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Allen P LiuBiophysics Program, University of California, Berkeley, CA 94720, USA.
Daniel A Fletcher
University of California, Berkeley · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The ability of cells to mount localized responses to external or internal stimuli is critically dependent on organization of lipids and proteins in the plasma membrane. Involvement of the actin cytoskeleton in membrane organization has been documented, but an active role for actin networks that directly links internal organization of the cytoskeleton with membrane organization has not yet been identified. Here we show that branched actin networks formed on model lipid membranes enriched with the lipid second messenger PIP(2) trigger both temporal and spatial rearrangement of membrane components. Using giant unilamellar vesicles able to separate into two coexisting liquid phases, we demonstrate that polymerization of dendritic actin networks on the membrane induces phase separation of initially homogenous vesicles. This switch-like behavior depends only on the PIP(2)-N-WASP link between the membrane and actin network, and we find that the presence of a preexisting actin network spatially biases the location of phase separation. These results show that dynamic, membrane-bound actin networks alone can control when and where membrane domains form and may actively contribute to membrane organization during cell signaling.

Indexed as

ActinsAnimalsCell MembraneCytoskeletonEscherichia coliLipid BilayersLipidsMicroscopy, ConfocalMicroscopy, FluorescenceMicroscopy, Phase-ContrastModels, MolecularPhosphatidylinositol 4,5-DiphosphateProtein Structure, TertiaryRatsWiskott-Aldrich Syndrome Protein, NeuronalActinsLipid BilayersLipidsPhosphatidylinositol 4,5-DiphosphateWiskott-Aldrich Syndrome Protein, Neuronal

Identifiers

PMID16963509
PMCPMC1635687
OpenAlexW1993544865

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.