Evidence map›Paper›PMID 19115233›Full record

ArticleJournal of cellular physiology2009

Loss of profilin-1 expression enhances breast cancer cell motility by Ena/VASP proteins.

Yong Ho Bae, Zhijie Ding, Li Zou, Alan Wells, Frank Gertler, Partha Roy

Open access · greenAbstract read
In one paragraph

Article in Journal of cellular physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.

0numbers the graph read from it
0cells of the map it votes in
56citing papers in PubMed
2.5field-weighted citation impact, top 11% 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

56 citing papers in PubMed, 89 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. SerFrontiers in cell and developmental biology · 2021
    Article
  9. Article
  10. Review
  11. Endometrial profilin 1: a key player in embryo-endometrial crosstalk.Clinical and experimental reproductive medicine · 2020
    Article
  12. Profilin choreographs actin and microtubules in cells and cancer.International review of cell and molecular biology · 2020
    Article
  13. Article
  14. Article
  15. Article
  16. Mutually inhibitory Ras-PI(3,4)PProceedings of the National Academy of Sciences of the United States of America · 2018
    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

6 authors at 2 institutions in 1 country.

Yong Ho BaeDepartment of Bioengineering, University of Pittsburgh, Pittsburgh, Pennsylvania 15219, USA.
Zhijie Ding
Li Zou
Alan Wells
Frank Gertler
Partha Roy
University of Pittsburgh · USMassachusetts Institute of Technology · US

Funding

VIRUS PRODUCTION COREP30CA014051 · NCI · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI MATTHEW G. VANDER HEIDEN · 1985 to 2026
$93.9M
CELLULAR AND DEVELOPMENTAL FUNCTIONS OF MENAR01GM058801 · NIGMS · MASSACHUSETTS INSTITUTE OF TECHNOLOGY · PI GERTLER, FRANK B · 1999 to 2012
$3.8M
Profilin as a target to suppress Invasive breast cancerR01CA108607 · NCI · UNIVERSITY OF PITTSBURGH AT PITTSBURGH · PI ROY, PARTHA · 2006 to 2017
$2.6M
NCI NIH HHS P30 CA014051NCI NIH HHS R01 CA108607NCI NIH HHS R01-CA108607NIGMS NIH HHS GM58801NIGMS NIH HHS R01 GM058801
6 · The paper itself

Abstract

We previously showed that silencing profilin-1 (Pfn1) expression increases breast cancer cell motility, but the underlying mechanisms have not been explored. Herein, we demonstrate that loss of Pfn1 expression leads to slower but more stable lamellipodial protrusion thereby enhancing the net protrusion rate and the overall motility of MDA-MB-231 breast cancer cells. Interestingly, MDA-MB-231 cells showed dramatic enrichment of VASP at their leading edge when Pfn1 expression was downregulated and this observation was also reproducible in other cell types including human mammary epithelial cells and vascular endothelial cells. We further demonstrate that Pfn1 downregulation results in a hyper-motile phenotype of MDA-MB-231 cells in an Ena/VASP-dependent mechanism. Pfn1-depleted cells display a strong colocalization of VASP with lamellipodin (Lpd--a PI(3,4)P(2)-binding protein that has been previously implicated in lamellipodial targeting of Ena/VASP) at the leading edge. Finally, inhibition of PI3-kinase (important for generation of PI(3,4)P(2)) delocalizes VASP from the leading edge. This observation is consistent with a possible involvement of Lpd in enhanced membrane recruitment of VASP that results from loss of Pfn1 expression. Our findings for the first time highlight a possible mechanism of how reduced expression of a pro-migratory molecule like Pfn1 could actually promote motility of breast cancer cells.

Indexed as

ActinsAnimalsBreast NeoplasmsCell Adhesion MoleculesCell LineCell MovementFemaleGene SilencingHumansMicrofilament ProteinsPhenotypePhosphoproteinsProfilinsPseudopodiaRNA, Small InterferingVasodilator-Stimulated PhosphoproteinActinsCell Adhesion MoleculesMicrofilament ProteinsPhosphoproteinsProfilinsRNA, Small InterferingVasodilator-Stimulated Phosphoprotein

Identifiers

PMID19115233
PMCPMC2990882
OpenAlexW2143844131

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.