Evidence map›Paper›PMID 25527498›Full record

ArticleThe Journal of biological chemistry2015

Rho GTPases and the downstream effectors actin-related protein 2/3 (Arp2/3) complex and myosin II induce membrane fusion at self-contacts.

Grant M Sumida, Soichiro Yamada

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
1.1field-weighted citation impact, top 27% 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

22 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Pathogen-Mediated Cell Fusion and Actin Cytoskeleton.Advances in experimental medicine and biology · 2026
    Review
  5. Article
  6. Review
  7. Article
  8. Article
  9. Functions of Arp2/3 Complex in the Dynamics of Epithelial Tissues.Frontiers in cell and developmental biology · 2022
    Review
  10. Frontiers in cellular and infection microbiology · 2022
    Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Review
  17. Article
  18. Changes in E-cadherin rigidity sensing regulate cell adhesion.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
  19. Time to make the doughnuts: Building and shaping seamless tubes.Seminars in cell & developmental biology · 2017
    Review
  20. Auto-fusion and the shaping of neurons and tubes.Seminars in cell & developmental biology · 2016
    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

2 authors at 1 institution in 1 country.

Grant M SumidaFrom the Department of Biomedical Engineering, University of California, Davis, California 95616.
Soichiro YamadaFrom the Department of Biomedical Engineering, University of California, Davis, California 95616 syamada@ucdavis.edu.
University of California, Davis · US

Funding

Cell adhesion mediated self-recognitionR01GM094798 · NIGMS · UNIVERSITY OF CALIFORNIA AT DAVIS · PI YAMADA, SOICHIRO · 2010 to 2013
$1.1M
NIGMS NIH HHS GM094798NIGMS NIH HHS R01 GM094798
6 · The paper itself

Abstract

Actin regulation is required for membrane activities that drive cell adhesion and migration. The Rho GTPase family plays critical roles in actin and membrane dynamics; however, the roles of the Rho GTPase family are not limited to cell adhesion and migration. Using micron-sized obstacles to induce the formation of self-contacts in epithelial cells, we previously showed that self-adhesion is distinct from cell-to-cell adhesion in that self-contacts are eliminated by membrane fusion. In the current study, we identified Rho GTPases, RhoA, Rac1, and Cdc42, as potential upstream regulators of membrane fusion. The RhoA downstream effector myosin II is required for fusion as the expression of mutant myosin light chain reduced membrane fusion. Furthermore, an inhibitor of the Arp2/3 complex, a downstream effector of Rac1 and Cdc42, also reduced self-contact-induced membrane fusion. At self-contacts, while the concentration of E-cadherin diminished, the intensity of GFP-tagged Arp3 rapidly fluctuated then decreased and stabilized after membrane fusion. Taken together, these data suggest that the Arp2/3 complex-mediated actin polymerization brings two opposing membranes into close apposition by possibly excluding E-cadherin from contact sites, thus promoting membrane fusion at self-contacts.

Indexed as

Membrane FusionActin-Related Protein 2Actin-Related Protein 3ActinsAnimalsCadherinscdc42 GTP-Binding ProteinDogsEpithelial CellsIntercellular JunctionsMadin Darby Canine Kidney CellsMyosin Type IIProtein Multimerizationrac1 GTP-Binding ProteinrhoA GTP-Binding ProteinActin-Related Protein 2Actin-Related Protein 3ActinsCadherinscdc42 GTP-Binding ProteinMyosin Type IIrac1 GTP-Binding ProteinrhoA GTP-Binding ProteinActinArp2/3 ComplexCadherin-1 (CDH1) (Epithelial Cadherin) (E-cadherin)Membrane FusionSmall GTPase

Identifiers

PMID25527498
PMCPMC4318998
OpenAlexW1967991256

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.