Evidence map›Paper›PMID 26639106›Full record

ArticleNature communications2015

Arp2/3-mediated F-actin formation controls regulated exocytosis in vivo.

Duy T Tran, Andrius Masedunskas, Roberto Weigert, Kelly G Ten Hagen

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 papers.

0numbers the graph read from it
0cells of the map it votes in
62citing papers in PubMed
5.2field-weighted citation impact, top 4% 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

62 citing papers in PubMed, 100 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
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  6. Article
  7. PI(4,5)PBiochimica et biophysica acta. Molecular and cell biology of lipids · 2025
    Review
  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Review
  14. Patterning of the cell cortex by Rho GTPases.Nature reviews. Molecular cell biology · 2024
    Review
  15. A novel cysteine-rich adaptor protein is required for mucin packaging and secretory granule stability in vivo.Proceedings of the National Academy of Sciences of the United States of America · 2024
    Article
  16. Article
  17. Article
  18. Article
  19. Regulated Restructuring of Mucins During Secretory Granule Maturation In Vivo.Proceedings of the National Academy of Sciences of the United States of America · 2022
    Article
  20. Review

2 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.

Duy T TranDevelopmental Glycobiology Section, NIDCR, National Institutes of Health, Building 30, Room 426, 30 Convent Drive, MSC 4370, Bethesda, Maryland 20892, USA.
Andrius MasedunskasIntracellular Membrane Trafficking Section, NIDCR, National Institutes of Health, 30 Convent Drive, Bethesda, Maryland 20892, USA.
Roberto WeigertIntracellular Membrane Trafficking Section, NIDCR, National Institutes of Health, 30 Convent Drive, Bethesda, Maryland 20892, USA.
Kelly G Ten HagenDevelopmental Glycobiology Section, NIDCR, National Institutes of Health, Building 30, Room 426, 30 Convent Drive, MSC 4370, Bethesda, Maryland 20892, USA.
National Institute of Dental and Craniofacial Research · USNational Institutes of Health · US

Funding

Role of O-glycosylation in Animal DevelopmentZIADE000713 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI TEN HAGEN, KELLY G · 2009 to 2025
$30.6M
Role of O-glycosylation in Animal DevelopmentZ01DE000713 · NIDCR · NATIONAL INSTITUTE OF DENTAL & CRANIOFACIAL RESEARCH · PI TEN HAGEN, KELLY G · 2006 to 2008
$2.0M
Intramural NIH HHS Z01 DE000713
6 · The paper itself

Abstract

The actin cytoskeleton plays crucial roles in many cellular processes, including regulated secretion. However, the mechanisms controlling F-actin dynamics in this process are largely unknown. Through 3D time-lapse imaging in a secreting organ, we show that F-actin is actively disassembled along the apical plasma membrane at the site of secretory vesicle fusion and re-assembled directionally on vesicle membranes. Moreover, we show that fusion pore formation and PIP2 redistribution precedes actin and myosin recruitment to secretory vesicle membranes. Finally, we show essential roles for the branched actin nucleators Arp2/3- and WASp in the process of secretory cargo expulsion and integration of vesicular membranes with the apical plasma membrane. Our results highlight previously unknown roles for branched actin in exocytosis and provide a genetically tractable system to image the temporal and spatial dynamics of polarized secretion in vivo.

Indexed as

ExocytosisActin CytoskeletonActin-Related Protein 2-3 ComplexActinsAnimalsCell MembraneCell PolarityDrosophilaDrosophila ProteinsImaging, Three-DimensionalMyosinsReal-Time Polymerase Chain ReactionSalivary GlandsSecretory VesiclesTime-Lapse ImagingWiskott-Aldrich Syndrome ProteinActin-Related Protein 2-3 ComplexActinsDrosophila ProteinsMyosinsWASp protein, DrosophilaWiskott-Aldrich Syndrome Protein

Identifiers

PMID26639106
PMCPMC4686765
OpenAlexW2193976754

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.