Evidence map›Paper›PMID 22357946›Full record

ArticleJournal of cell science2012

VANGL2 regulates membrane trafficking of MMP14 to control cell polarity and migration.

B Blairanne Williams, V Ashley Cantrell, Nathan A Mundell, Andrea C Bennett, Rachel E Quick, Jason R Jessen

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 39 papers.

0numbers the graph read from it
0cells of the map it votes in
39citing papers in PubMed
3.5field-weighted citation impact, top 7% 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

39 citing papers in PubMed, 70 citations in OpenAlex.

  1. Article
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  6. Vanadium Modulates Proteolytic Activities and MMP-14-Like Levels duringInternational journal of molecular sciences · 2022
    Article
  7. Review
  8. Wnt signaling in biliary development, proliferation, and fibrosis.Experimental biology and medicine (Maywood, N.J.) · 2022
    Review
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  14. Article
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  19. Article
  20. The role of polarisation of circulating tumour cells in cancer metastasis.Cellular and molecular life sciences : CMLS · 2019
    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

6 authors at 1 institution in 1 country.

B Blairanne WilliamsDivision of Genetic Medicine/Department of Medicine, Vanderbilt University Medical Center, Nashville, TN 37232, USA.
V Ashley Cantrell
Nathan A Mundell
Andrea C Bennett
Rachel E Quick
Jason R Jessen
Vanderbilt University Medical Center · US

Funding

Tumor Immunology and Microenvironment Research ProgramP30CA068485 · NCI · VANDERBILT UNIVERSITY MEDICAL CENTER · PI MATTHEW J TYSKA · 1995 to 2026
$172.8M
NCI NIH HHS P30 CA068485
6 · The paper itself

Abstract

Planar cell polarity (PCP) describes the polarized orientation of cells within the plane of a tissue. Unlike epithelial PCP, the mechanisms underlying PCP signaling in migrating cells remain undefined. Here, the establishment of PCP must be coordinated with dynamic changes in cell adhesion and extracellular matrix (ECM) organization. During gastrulation, the membrane type-1 matrix metalloproteinase (MT1-MMP or MMP14) is required for PCP and convergence and extension cell movements. We report that the PCP protein Vang-like 2 (VANGL2) regulates the endocytosis and cell-surface availability of MMP14 in manner that is dependent on focal adhesion kinase. We demonstrate that zebrafish trilobite/vangl2 mutant embryos exhibit increased Mmp14 activity and decreased ECM. Furthermore, in vivo knockdown of Mmp14 partially rescues the Vangl2 loss-of-function convergence and extension phenotype. This study identifies a mechanism linking VANGL2 with MMP14 trafficking and suggests that establishment of PCP in migrating gastrula cells requires regulated proteolytic degradation or remodeling of the ECM. Our findings implicate matrix metalloproteinases as downstream effectors of PCP and suggest a broadly applicable mechanism whereby VANGL2 affects diverse morphogenetic processes.

Indexed as

AnimalsCell AdhesionCell MembraneCell MovementCell PolarityEmbryo, NonmammalianEndocytosisExtracellular MatrixFocal Adhesion Protein-Tyrosine KinasesGastrulaGastrulationGene Knockdown TechniquesMatrix Metalloproteinase 14Membrane ProteinsMutationProtein TransportFocal Adhesion Protein-Tyrosine KinasesMatrix Metalloproteinase 14Membrane Proteinsvangl2 protein, zebrafishZebrafish Proteins

Identifiers

PMID22357946
PMCPMC3367937
OpenAlexW2027275365

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.