Evidence map›Paper›PMID 25963656›Full record

ArticleMolecular and cellular biology2015

Rap1 Spatially Controls ArhGAP29 To Inhibit Rho Signaling during Endothelial Barrier Regulation.

A Post, W J Pannekoek, B Ponsioen, M J Vliem, J L Bos

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
5.0field-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

49 citing papers in PubMed, 86 citations in OpenAlex.

  1. Article
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  4. Review
  5. Article
  6. ARHGAP29 promotes keratinocyte proliferation and migration in vitro and is dispensable for in vivo wound healing.Developmental dynamics : an official publication of the American Association of Anatomists · 2025
    Article
  7. Article
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  10. Molecular Mechanisms Regulating Vascular Endothelial Permeability.International journal of molecular sciences · 2024
    Review
  11. Article
  12. Article
  13. Spatial Mechano-Signaling Regulation of GTPases through Non-Degradative Ubiquitination.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2023
    Article
  14. Article
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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

5 authors at 2 institutions in 1 country.

A PostMolecular Cancer Research and Cancer Genomics Netherlands, Center for Molecular Medicine, University Medical Center Utrecht, Utrecht, The Netherlands.
W J PannekoekMolecular Cancer Research and Cancer Genomics Netherlands, Center for Molecular Medicine, University Medical Center Utrecht, Utrecht, The Netherlands.
B PonsioenMolecular Cancer Research and Cancer Genomics Netherlands, Center for Molecular Medicine, University Medical Center Utrecht, Utrecht, The Netherlands.
M J VliemMolecular Cancer Research and Cancer Genomics Netherlands, Center for Molecular Medicine, University Medical Center Utrecht, Utrecht, The Netherlands.
J L BosMolecular Cancer Research and Cancer Genomics Netherlands, Center for Molecular Medicine, University Medical Center Utrecht, Utrecht, The Netherlands j.l.bos@umcutrecht.nl.
Cancer Genomics Centre · NLUniversity Medical Center Utrecht · NL

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The small GTPase Rap1 controls the actin cytoskeleton by regulating Rho GTPase signaling. We recently established that the Rap1 effectors Radil and Rasip1, together with the Rho GTPase activating protein ArhGAP29, mediate Rap1-induced inhibition of Rho signaling in the processes of epithelial cell spreading and endothelial barrier function. Here, we show that Rap1 induces the independent translocations of Rasip1 and a Radil-ArhGAP29 complex to the plasma membrane. This results in the formation of a multimeric protein complex required for Rap1-induced inhibition of Rho signaling and increased endothelial barrier function. Together with the previously reported spatiotemporal control of the Rap guanine nucleotide exchange factor Epac1, these findings elucidate a signaling pathway for spatiotemporal control of Rho signaling that operates by successive protein translocations to and complex formation at the plasma membrane.

Indexed as

Signal TransductionCarrier ProteinsCells, CulturedGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsHEK293 CellsHumansHuman Umbilical Vein Endothelial CellsIntercellular JunctionsIntracellular Signaling Peptides and ProteinsLuminescent ProteinsMicroscopy, ConfocalProtein BindingProtein Transportrap1 GTP-Binding Proteinsrho GTP-Binding ProteinsARHGAP29 protein, humanCarrier ProteinsGTPase-Activating ProteinsGuanine Nucleotide Exchange FactorsIntracellular Signaling Peptides and ProteinsLuminescent ProteinsRADIL protein, humanrap1 GTP-Binding ProteinsRAPGEF3 protein, humanRASIP1 protein, humanrho GTP-Binding Proteins

Identifiers

PMID25963656
PMCPMC4475929
OpenAlexW1905949153

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.