Evidence map›Paper›PMID 20829485›Full record

ArticleScience (New York, N.Y.)2010

Self-assembly of filopodia-like structures on supported lipid bilayers.

Kwonmoo Lee, Jennifer L Gallop, Komal Rambani, Marc W Kirschner

Open access · greenAbstract read
In one paragraph

Article in Science (New York, N.Y.), 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
7.3field-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

84 citing papers in PubMed, 166 citations in OpenAlex.

  1. Emerging Roles of Cytoneme-Mediated Signaling in Cancer.International journal of molecular sciences · 2026
    Review
  2. Article
  3. The actin assembly regulatorbioRxiv : the preprint server for biology · 2025
    Article
  4. Article
  5. Review
  6. Article
  7. The role of actin cytoskeleton component Arp2/3 in inflammatory response.Frontiers in cell and developmental biology · 2025
    Review
  8. Article
  9. Interpretable Fine-Grained Phenotypes of Subcellular Dynamics via Unsupervised Deep Learning.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Article
  10. Article
  11. Article
  12. Article
  13. Competition and Synergy of Arp2/3 and Formins in Nucleating Actin Waves.bioRxiv : the preprint server for biology · 2023
    Article
  14. Article
  15. 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
  16. Article
  17. Article
  18. Article
  19. Regulatory mechanisms of cytoneme-based morphogen transport.Cellular and molecular life sciences : CMLS · 2022
    Review
  20. Dendrite tapering actuates a self-organizing signaling circuit for stochastic filopodia initiation in neurons.Proceedings of the National Academy of Sciences of the United States of America · 2021
    Article

24 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 at 2 institutions in 1 country.

Kwonmoo LeeDepartment of Systems Biology, Harvard Medical School, Boston, MA 02115, USA.
Jennifer L Gallop
Komal Rambani
Marc W Kirschner
Center for Systems Biology · USHarvard University · US

Funding

BIOCHEMICAL STUDIES OF MITOSISR01GM026875 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI KIRSCHNER, MARC WALLACE · 1985 to 2019
$18.2M
BIOCHEMICAL STUDIES OF MITOSISR37GM026875 · NIGMS · UNIVERSITY OF CALIFORNIA SAN FRANCISCO · PI KIRSCHNER, MARC W · 1986 to 1995
–
NIGMS NIH HHS GM26875NIGMS NIH HHS R01 GM026875
6 · The paper itself

Abstract

Filopodia are finger-like protrusive structures, containing actin bundles. By incubating frog egg extracts with supported lipid bilayers containing phosphatidylinositol 4,5 bisphosphate, we have reconstituted the assembly of filopodia-like structures (FLSs). The actin assembles into parallel bundles, and known filopodial components localize to the tip and shaft. The filopodia tip complexes self-organize--they are not templated by preexisting membrane microdomains. The F-BAR domain protein toca-1 recruits N-WASP, followed by the Arp2/3 complex and actin. Elongation proteins, Diaphanous-related formin, VASP, and fascin are recruited subsequently. Although the Arp2/3 complex is required for FLS initiation, it is not essential for elongation, which involves formins. We propose that filopodia form via clustering of Arp2/3 complex activators, self-assembly of filopodial tip complexes on the membrane, and outgrowth of actin bundles.

Indexed as

Lipid BilayersActin CytoskeletonActin-Related Protein 2-3 ComplexActinsAnimalsCarrier ProteinsCell Adhesion MoleculesCell MembraneHumansKineticsMembrane MicrodomainsMiceMicrofilament ProteinsMicrotubule-Associated ProteinsNADPH DehydrogenasePhosphatidylinositol PhosphatesActin-Related Protein 2-3 ComplexActinsCarrier ProteinsCell Adhesion MoleculesDia2 protein, mousefascinFNBP1L protein, humanLipid BilayersMicrofilament ProteinsMicrotubule-Associated ProteinsNADPH DehydrogenasePhosphatidylinositol PhosphatesPhosphoproteinsRecombinant Fusion ProteinsVasodilator-Stimulated PhosphoproteinWiskott-Aldrich Syndrome Protein, NeuronalXenopus Proteins

Identifiers

PMID20829485
PMCPMC2982780
OpenAlexW2065868796

What OpenQuestion holds

Textmetadata
LicenceTDM
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.