Evidence map›Paper›PMID 27116935›Full record

ArticleScientific reports2016

LIMK Regulates Tumor-Cell Invasion and Matrix Degradation Through Tyrosine Phosphorylation of MT1-MMP.

Emilie Lagoutte, Clémentine Villeneuve, Laurence Lafanechère, Claire M Wells, Gareth E Jones, Philippe Chavrier, Carine Rossé

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.

0numbers the graph read from it
0cells of the map it votes in
47citing papers in PubMed
3.8field-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

47 citing papers in PubMed, 69 citations in OpenAlex.

  1. Article
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  4. Regulation and signaling of the LIM domain kinases.BioEssays : news and reviews in molecular, cellular and developmental biology · 2025
    Review
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  9. Cytoplasmic Tail of MT1-MMP: A Hub of MT1-MMP Regulation and Function.International journal of molecular sciences · 2023
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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

7 authors at 3 institutions in 2 countries.

Emilie LagoutteInstitut Curie, PSL Research University, CNRS UMR 144, Membrane and Cytoskeleton Dynamics, 75248 cedex 05, Paris, France.
Clémentine VilleneuveInstitut Curie, PSL Research University, CNRS UMR 144, Membrane and Cytoskeleton Dynamics, 75248 cedex 05, Paris, France.
Laurence LafanechèreUniv. Grenoble Alpes, INSERM U823, Institut Albert Bonniot, CRI, Team 3 "Polarity, Development and Cancer", F-38000 Grenoble France.
Claire M WellsDivision of Cancer Studies, King's College London, London, United Kingdom.
Gareth E JonesRandall Division of Cell and Molecular Biophysics, King's College London, London, United Kingdom.
Philippe ChavrierInstitut Curie, PSL Research University, CNRS UMR 144, Membrane and Cytoskeleton Dynamics, 75248 cedex 05, Paris, France.
Carine RosséInstitut Curie, PSL Research University, CNRS UMR 144, Membrane and Cytoskeleton Dynamics, 75248 cedex 05, Paris, France.
Centre National de la Recherche Scientifique · FRKing's College London · GBInserm · FR

Funding

Medical Research Council G1100041
6 · The paper itself

Abstract

During their metastatic spread, cancer cells need to remodel the extracellular matrix in order to migrate through stromal compartments adjacent to the primary tumor. Dissemination of breast carcinoma cells is mediated by membrane type 1-matrix metalloproteinase (MT1-MMP/MMP14), the main invadopodial matrix degradative component. Here, we identify MT1-MMP as a novel interacting partner of dual-specificity LIM Kinase-1 and -2 (LIMK1/2), and provide several evidence for phosphorylation of tyrosine Y573 in the cytoplasmic domain of MT1-MMP by LIMK. Phosphorylation of Y573 influences association of F-actin binding protein cortactin to MT1-MMP-positive endosomes and invadopodia formation and matrix degradation. Moreover, we show that LIMK1 regulates cortactin association to MT1-MMP-positive endosomes, while LIMK2 controls invadopodia-associated cortactin. In turn, LIMK1 and LIMK2 are required for MT1-MMP-dependent matrix degradation and cell invasion in a three-dimensional type I collagen environment. This novel link between LIMK1/2 and MT1-MMP may have important consequences for therapeutic control of breast cancer cell invasion.

Indexed as

Cell MovementProtein Processing, Post-TranslationalCell Line, TumorCortactinHumansLim KinasesMatrix Metalloproteinase 14PhosphorylationProtein BindingProtein Interaction MappingTyrosineCortactinCTTN protein, humanLIMK1 protein, humanLIMK2 protein, humanLim KinasesMatrix Metalloproteinase 14Tyrosine

Identifiers

PMID27116935
PMCPMC4847008
OpenAlexW2342485854

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.