Evidence map›Paper›PMID 27069022›Full record

ArticleThe Journal of cell biology2016

Metalloproteinase MT1-MMP islets act as memory devices for podosome reemergence.

Karim El Azzouzi, Christiane Wiesner, Stefan Linder

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
5.3field-weighted citation impact, top 4% 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

31 citing papers in PubMed, 63 citations in OpenAlex.

  1. Article
  2. Podosomes and Mechanical Force.Results and problems in cell differentiation · 2026
    Review
  3. Macrophage Actin Cytoskeleton in Chronic Rejection.Results and problems in cell differentiation · 2026
    Review
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Novel Roles of MT1-MMP and MMP-2: Beyond the Extracellular Milieu.International journal of molecular sciences · 2022
    Review
  11. Review
  12. Regulatory mechanism of oral mucosal rete peg formation.Journal of molecular histology · 2021
    Review
  13. Tissue remodeling by invadosomes.Faculty reviews · 2021
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  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

3 authors at 2 institutions in 1 country.

Karim El AzzouziInstitut für medizinische Mikrobiologie, Virologie und Hygiene, Universitätsklinikum Eppendorf, 20246 Hamburg, Germany.
Christiane WiesnerInstitut für medizinische Mikrobiologie, Virologie und Hygiene, Universitätsklinikum Eppendorf, 20246 Hamburg, Germany.
Stefan LinderInstitut für medizinische Mikrobiologie, Virologie und Hygiene, Universitätsklinikum Eppendorf, 20246 Hamburg, Germany s.linder@uke.de.
Universität Hamburg · DEUniversity Medical Center Hamburg-Eppendorf · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Podosomes are dynamic cell adhesions that are also sites of extracellular matrix degradation, through recruitment of matrix-lytic enzymes, particularly of matrix metalloproteinases. Using total internal reflection fluorescence microscopy, we show that the membrane-bound metalloproteinase MT1-MMP is enriched not only at podosomes but also at distinct "islets" embedded in the plasma membrane of primary human macrophages. MT1-MMP islets become apparent upon podosome dissolution and persist beyond podosome lifetime. Importantly, the majority of MT1-MMP islets are reused as sites of podosome reemergence. siRNA-mediated knockdown and recomplementation analyses show that islet formation is based on the cytoplasmic tail of MT1-MMP and its ability to bind the subcortical actin cytoskeleton. Collectively, our data reveal a previously unrecognized phase in the podosome life cycle and identify a structural function of MT1-MMP that is independent of its proteolytic activity. MT1-MMP islets thus act as cellular memory devices that enable efficient and localized reformation of podosomes, ensuring coordinated matrix degradation and invasion.

Indexed as

Actin CytoskeletonCell MembraneCell MovementCells, CulturedExtracellular MatrixHumansMacrophagesMatrix Metalloproteinase 14Matrix MetalloproteinasesPodosomesRNA, Small InterferingMatrix Metalloproteinase 14Matrix MetalloproteinasesMMP14 protein, humanRNA, Small Interfering

Identifiers

PMID27069022
PMCPMC4828691
OpenAlexW2324571563

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.