Evidence map›Paper›PMID 24807903›Full record

ArticleMolecular biology of the cell2014

SNAP23, Syntaxin4, and vesicle-associated membrane protein 7 (VAMP7) mediate trafficking of membrane type 1-matrix metalloproteinase (MT1-MMP) during invadopodium formation and tumor cell invasion.

Karla C Williams, Rachael E McNeilly, Marc G Coppolino

Abstract read
In one paragraph

Article in Molecular biology of the cell, 2014. 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
3.0field-weighted citation impact, top 9% 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, 94 citations in OpenAlex.

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  13. Tumor TargetingMicroRNA (Shariqah, United Arab Emirates) · 2024
    Article
  14. Article
  15. Cytoplasmic Tail of MT1-MMP: A Hub of MT1-MMP Regulation and Function.International journal of molecular sciences · 2023
    Review
  16. Spatial organization of lysosomal exocytosis relies on membrane tension gradients.Proceedings of the National Academy of Sciences of the United States of America · 2023
    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

3 authors at 1 institution in 1 country.

Karla C WilliamsDepartment of Molecular and Cellular Biology, University of Guelph, Guelph, ON N1G 2W1, Canada.
Rachael E McNeillyDepartment of Molecular and Cellular Biology, University of Guelph, Guelph, ON N1G 2W1, Canada.
Marc G CoppolinoDepartment of Molecular and Cellular Biology, University of Guelph, Guelph, ON N1G 2W1, Canada mcoppoli@uoguelph.ca.
University of Guelph · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Movement through the extracellular matrix (ECM) requires cells to degrade ECM components, primarily through the action of matrix metalloproteinases (MMPs). Membrane type 1-matrix metalloproteinase (MT1-MMP) has an essential role in matrix degradation and cell invasion and localizes to subcellular degradative structures termed invadopodia. Trafficking of MT1-MMP to invadopodia is required for the function of these structures, and here we examine the role of N-ethylmaleimide-sensitive factor-activating protein receptor (SNARE)-mediated membrane traffic in the transport of MT1-MMP to invadopodia. During invadopodium formation in MDA-MB-231 human breast cancer cells, increased association of SNAP23, Syntaxin4, and vesicle-associated membrane protein 7 (VAMP7) is detected by coimmunoprecipitation. Blocking the function of these SNAREs perturbs invadopodium-based ECM degradation and cell invasion. Increased level of SNAP23-Syntaxin4-VAMP7 interaction correlates with decreased Syntaxin4 phosphorylation. These results reveal an important role for SNARE-regulated trafficking of MT1-MMP to invadopodia during cellular invasion of ECM.

Indexed as

Cell Line, TumorCell Surface ExtensionsExtracellular MatrixHumansMatrix Metalloproteinase 14Neoplasm InvasivenessProtein TransportQa-SNARE ProteinsQb-SNARE ProteinsQc-SNARE ProteinsR-SNARE ProteinsMatrix Metalloproteinase 14MMP14 protein, humanQa-SNARE ProteinsQb-SNARE ProteinsQc-SNARE ProteinsR-SNARE ProteinsSNAP23 protein, humansyntaxin 4, humanVAMP7 protein, human

Identifiers

PMID24807903
PMCPMC4072579
OpenAlexW2134562563

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.