Evidence map›Paper›PMID 17942688›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2007

ARF1-mediated actin polymerization produces movement of artificial vesicles.

Julien Heuvingh, Michel Franco, Philippe Chavrier, Cécile Sykes

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
2.6field-weighted citation impact, top 12% 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

20 citing papers in PubMed, 42 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Actin acting at the Golgi.Histochemistry and cell biology · 2013
    Review
  8. Article
  9. Actin polymerization or myosin contraction: two ways to build up cortical tension for symmetry breaking.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2013
    Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Small-molecule p21-activated kinase inhibitor PF-3758309 is a potent inhibitor of oncogenic signaling and tumor growth.Proceedings of the National Academy of Sciences of the United States of America · 2010
    Article
  15. Article
  16. Article
  17. How cofilin severs an actin filament.Biophysical reviews · 2009
    Article
  18. Spatial Segregation of Phosphatidylinositol 4,5-Bisphosphate (PIP(2)) Signaling in Immune Cell Functions.Immunology, endocrine & metabolic agents in medicinal chemistry · 2008
    Article
  19. Article
  20. Article
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.

Julien HeuvinghCentre de Recherche, Institut Curie, F-75248 Paris, France.
Michel Franco
Philippe Chavrier
Cécile Sykes
Institut Curie · FRCentre National de la Recherche Scientifique · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Vesicular trafficking and actin dynamics on Golgi membranes are both regulated by ADP-ribosylation factor 1 (ARF1) through the recruitment of various effectors, including vesicular coats. Actin assembly on Golgi membranes contributes to the architecture of the Golgi complex, vesicle formation, and trafficking and is mediated by ARF1 through a cascade that leads to Arp2/3 complex activation. Here we addressed the role of Golgi actin downstream of ARF1 by using a biomimetic assay consisting of liposomes of defined lipid composition, carrying an activated form of ARF1 incubated in cytosolic cell extracts. We observed actin polymerization around the liposomes resulting in thick actin shells and actin comet tails that pushed the ARF1 liposomes forward. The assay was used to characterize the ARF1-dependent pathway, leading to actin polymerization, and confirmed a dependency on CDC42 and its downstream effector N-WASP. Overall, this study demonstrates that actin polymerization driven by the complex multicomponent signaling cascade of the Golgi apparatus can be reproduced with a biomimetic system. Moreover, our results are consistent with the view that actin-based force generation at the site of vesicle formation contributes to the mechanism of fission. In addition to its well established function in coat recruitment, the ARF1 machinery also might produce movement- and fission-promoting forces through actin polymerization.

Indexed as

ActinsADP-Ribosylation Factor 1AnimalsBiological TransportCattlecdc42 GTP-Binding ProteinCell MembraneGuanosine TriphosphateHeLa CellsHumansRabbitsUnilamellar LiposomesWiskott-Aldrich Syndrome Protein, NeuronalActinsADP-Ribosylation Factor 1cdc42 GTP-Binding ProteinGuanosine TriphosphateUnilamellar LiposomesWiskott-Aldrich Syndrome Protein, Neuronal

Identifiers

PMID17942688
PMCPMC2040406
OpenAlexW1980024120

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.