Evidence map›Paper›PMID 19158396›Full record

ArticleMolecular biology of the cell2009

The dioxin receptor regulates the constitutive expression of the vav3 proto-oncogene and modulates cell shape and adhesion.

Jose M Carvajal-Gonzalez, Sonia Mulero-Navarro, Angel Carlos Roman, Vincent Sauzeau, Jaime M Merino, Xose R Bustelo, Pedro M Fernandez-Salguero

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
–field-weighted citation impact
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

38 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Review
  8. Article
  9. Article
  10. Environmental chemicals, breast cancer progression and drug resistance.Environmental health : a global access science source · 2020
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. 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

7 authors.

Jose M Carvajal-GonzalezDepartamento de Bioquímica y Biología Molecular, Facultad de Ciencias, Universidad de Extremadura, 06071 Badajoz, Spain.
Sonia Mulero-Navarro
Angel Carlos Roman
Vincent Sauzeau
Jaime M Merino
Xose R Bustelo
Pedro M Fernandez-Salguero

Funding

VAV FAMILY PROTEINS IN CELL SIGNALING AND CANCERR01CA073735 · NCI · UNIVERSITY OF SALAMANCA · PI BUSTELO, XOSE R · 1997 to 2009
$1.8M
NCI NIH HHS 5R01-CA73735-11NCI NIH HHS R01 CA073735
6 · The paper itself

Abstract

The dioxin receptor (AhR) modulates cell plasticity and migration, although the signaling involved remains unknown. Here, we report a mechanism that integrates AhR into these cytoskeleton-related functions. Immortalized and mouse embryonic fibroblasts lacking AhR (AhR-/-) had increased cell area due to spread cytoplasms that reverted to wild-type morphology upon AhR re-expression. The AhR-null phenotype included increased F-actin stress fibers, depolarized focal adhesions, and enhanced spreading and adhesion. The cytoskeleton alterations of AhR-/- cells were due to down-regulation of constitutive Vav3 expression, a guanosine diphosphate/guanosine triphosphate exchange factor for Rho/Rac GTPases and a novel transcriptional target of AhR. AhR was recruited to the vav3 promoter and maintained constitutive mRNA expression in a ligand-independent manner. Consistently, AhR-/- fibroblasts had reduced Rac1 activity and increased activation of the RhoA/Rho kinase (Rock) pathway. Pharmacological inhibition of Rac1 shifted AhR+/+ fibroblasts to the null phenotype, whereas Rock inhibition changed AhR-null cells to the AhR+/+ morphology. Knockdown of vav3 transcripts by small interfering RNA induced cytoskeleton defects and changes in adhesion and spreading mimicking those of AhR-null cells. Moreover, vav3-/- MEFs, as AhR-/- mouse embryonic fibroblasts, had increased cell area and enhanced stress fibers. By modulating Vav3-dependent signaling, AhR could regulate cell shape, adhesion, and migration under physiological conditions and, perhaps, in certain pathological states.

Indexed as

Cell ShapeActinsAnimalsCell AdhesionCells, CulturedCytoskeletonMiceMice, KnockoutPhenotypeProto-Oncogene Proteins c-vavrac1 GTP-Binding ProteinReceptors, Aryl HydrocarbonrhoA GTP-Binding ProteinRNA, MessengerTranscription, GeneticActinsProto-Oncogene Proteins c-vavrac1 GTP-Binding ProteinReceptors, Aryl HydrocarbonrhoA GTP-Binding ProteinRNA, MessengerVav3 protein, mouse

Identifiers

PMID19158396
PMCPMC2655264

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.