Evidence map›Paper›PMID 24916416›Full record

ArticleCytoskeleton (Hoboken, N.J.)2014

Arf1 and Arf6 promote ventral actin structures formed by acute activation of protein kinase C and Src.

Juliane P Caviston, Lee Ann Cohen, Julie G Donaldson

Open access · hybridAbstract read
In one paragraph

Article in Cytoskeleton (Hoboken, N.J.), 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.

0numbers the graph read from it
0cells of the map it votes in
12citing papers in PubMed
1.5field-weighted citation impact, top 19% 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

12 citing papers in PubMed, 14 citations in OpenAlex.

  1. Article
  2. Review
  3. Macropinosome formation, maturation and membrane recycling: lessons from clathrin-independent endosomal membrane systems.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2019
    Article
  4. Arf GAPs as Regulators of the Actin Cytoskeleton-An Update.International journal of molecular sciences · 2019
    Review
  5. Article
  6. Article
  7. Endocytosis of Wingless via a dynamin-independent pathway is necessary for signaling inProceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  8. Review
  9. Article
  10. Article
  11. Article
  12. 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

3 authors at 1 institution in 1 country.

Juliane P CavistonCell Biology and Physiology Center, NHLBI, NIH, Bethesda, Maryland.
Lee Ann Cohen
Julie G Donaldson
National Institutes of Health · US

Funding

Light Microscopy CoreZICHL006019 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI COMBS, CHRISTIAN · 2009 to 2025
$29.3M
CELLULAR FUNCTION OF THE ADP-RIBOSYLATION FACTOR 6 GTP BINDING PROTEINZ01HL000517 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI DONALDSON, JULIE G · 1996 to 2008
$3.2M
Arf GTP-binding proteins and membrane trafficZIAHL000517 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI DONALDSON, JULIE G · 2009 to 2016
$2.6M
Intramural NIH HHS Z01 HL000517
6 · The paper itself

Abstract

Arf proteins regulate membrane traffic and organelle structure. Although Arf6 is known to initiate actin-based changes in cell surface architecture, Arf1 may also function at the plasma membrane. Here we show that acute activation of protein kinase C (PKC) induced by the phorbol ester PMA led to the formation of motile actin structures on the ventral surface of Beas-2b cells, a lung bronchial epithelial cell line. Ventral actin structures also formed in PMA-treated HeLa cells that had elevated levels of Arf activation. For both cell types, formation of the ventral actin structures was enhanced by expression of active forms of either Arf1 or Arf6 and by the expression of guanine nucleotide exchange factors that activate these Arfs. By contrast, formation of these structures was blocked by inhibitors of PKC and Src and required phosphatidylinositol 4, 5-bisphosphate, Rac, Arf6, and Arf1. Furthermore, expression of ASAP1, an Arf1 GTPase activating protein (GAP) was more effective at inhibiting the ventral actin structures than was ACAP1, an Arf6 GAP. This study adds to the expanding role for Arf1 in the periphery and identifies a requirement for Arf1, a "Golgi Arf," in the reorganization of the cortical actin cytoskeleton on ventral surfaces, against the substratum.

Indexed as

ActinsADP-Ribosylation Factor 1ADP-Ribosylation Factor 6ADP-Ribosylation FactorsBronchiCell LineCytoskeletonEnzyme ActivationHeLa CellsHumansProtein Kinase Csrc-Family KinasesActinsADP-Ribosylation Factor 1ADP-Ribosylation Factor 6ADP-Ribosylation FactorsARF6 protein, humanProtein Kinase Csrc-Family KinasesArf1cortical actinPKCSrcventral surface

Identifiers

PMID24916416
PMCPMC4711933
OpenAlexW2127593165

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.