Evidence map›Paper›PMID 11160830›Full record

ArticleMolecular biology of the cell2001

ATP-dependent membrane assembly of F-actin facilitates membrane fusion.

A Jahraus, M Egeberg, B Hinner, A Habermann, E Sackman, A Pralle, H Faulstich, V Rybin, H Defacque, G Griffiths

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2001. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 48 papers.

0numbers the graph read from it
0cells of the map it votes in
48citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

48 citing papers in PubMed, 113 citations in OpenAlex.

  1. Article
  2. Article
  3. Biophysical Considerations in Cell Fusion.Advances in experimental medicine and biology · 2026
    Review
  4. Review
  5. Article
  6. Assays of Platelet SNARE-actin Interactions.Methods in molecular biology (Clifton, N.J.) · 2025
    Article
  7. Article
  8. Article
  9. The ATP-dependent Pathways and Human Diseases.Current medicinal chemistry · 2023
    Article
  10. Review
  11. Article
  12. Review
  13. Article
  14. Leptin signaling impairs macrophage defenses againstProceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  15. Article
  16. Phosphatidylinositol 4-phosphate and phosphatidylinositol 3-phosphate regulate phagolysosome biogenesis.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Article
  18. Article
  19. Article
  20. Endosome maturation.The EMBO journal · 2011
    Review
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

10 authors at 3 institutions in 1 country.

A JahrausEuropean Molecular Biology Laboratory, Heidelberg, Germany.
M Egeberg
B Hinner
A Habermann
E Sackman
A Pralle
H Faulstich
V Rybin
H Defacque
G Griffiths
European Molecular Biology Laboratory · DETechnical University of Munich · DEMax Planck Institute for Medical Research · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We recently established an in vitro assay that monitors the fusion between latex-bead phagosomes and endocytic organelles in the presence of J774 macrophage cytosol (). Here, we show that different reagents affecting the actin cytoskeleton can either inhibit or stimulate this fusion process. Because the membranes of purified phagosomes can assemble F-actin de novo from pure actin with ATP (), we focused here on the ability of membranes to nucleate actin in the presence of J774 cytosolic extracts. For this, we used F-actin sedimentation, pyrene actin assays, and torsional rheometry, a biophysical approach that could provide kinetic information on actin polymerization and gel formation. We make two major conclusions. First, under our standard in vitro conditions (4 mg/ml cytosol and 1 mM ATP), the presence of membranes actively catalyzed the assembly of cytosolic F-actin, which assembled into highly viscoelastic gels. A model is discussed that links these results to how the actin may facilitate fusion. Second, cytosolic actin paradoxically polymerized more under ATP depletion than under high-ATP conditions, even in the absence of membranes; we discuss these data in the context of the well described, large increases in F-actin seen in many cells during ischemia.

Indexed as

ActinsAdenosine TriphosphateAnimalsBridged Bicyclo Compounds, HeterocyclicCell LineCytochalasin DCytoplasmEndosomesIntracellular MembranesKineticsMacrophagesMembrane FusionMicePhagosomesRheologyThiazolesActinsAdenosine TriphosphateBridged Bicyclo Compounds, HeterocyclicCytochalasin Dlatrunculin AThiazolesThiazolidines

Identifiers

PMID11160830
PMCPMC30575
OpenAlexW2132464310

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.