Evidence map›Paper›PMID 29061881›Full record

ArticleJournal of cell science2017

E-cadherin cleavage by MT2-MMP regulates apical junctional signaling and epithelial homeostasis in the intestine.

Jesús Gómez-Escudero, Vanessa Moreno, Mara Martín-Alonso, M Victoria Hernández-Riquer, Tamar Feinberg, Ángel Colmenar, Enrique Calvo, Emilio Camafeita, Fernando Martínez, Menno J Oudhoff and 2 more

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
1.2field-weighted citation impact, top 21% 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

15 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Review
  4. Article
  5. Article
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  8. Article
  9. Matrix Metalloproteinases inInternational journal of molecular sciences · 2022
    Review
  10. Mapping transmembrane binding partners for E-cadherin ectodomains.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  11. Article
  12. Article
  13. Article
  14. Review
  15. 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

12 authors at 3 institutions in 3 countries.

Jesús Gómez-EscuderoMatrix Metalloproteinases in Angiogenesis and Inflammation Group, Centro Nacional de Investigaciones Cardiovasculares Carlos III (CNIC), 28029 Madrid, Spain.
Vanessa MorenoMatrix Metalloproteinases in Angiogenesis and Inflammation Group, Centro Nacional de Investigaciones Cardiovasculares Carlos III (CNIC), 28029 Madrid, Spain.
Mara Martín-AlonsoCentre of Molecular Inflammation Research (CEMIR), Department of Clinical and Molecular Medicine, Faculty of Medicine and Health Sciences, Norwegian University of Science and Technology, 7491 Trondheim, Norway.
M Victoria Hernández-RiquerMatrix Metalloproteinases in Angiogenesis and Inflammation Group, Centro Nacional de Investigaciones Cardiovasculares Carlos III (CNIC), 28029 Madrid, Spain.
Tamar FeinbergDivision of Molecular Medicine and Genetics, Department of Internal Medicine, Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.
Ángel ColmenarMatrix Metalloproteinases in Angiogenesis and Inflammation Group, Centro Nacional de Investigaciones Cardiovasculares Carlos III (CNIC), 28029 Madrid, Spain.
Enrique CalvoProteomics Unit, Centro Nacional de Investigaciones Cardiovasculares Carlos III (CNIC), 28029 Madrid, Spain.
Emilio CamafeitaProteomics Unit, Centro Nacional de Investigaciones Cardiovasculares Carlos III (CNIC), 28029 Madrid, Spain.
Fernando MartínezBioinformatics Unit, Centro Nacional de Investigaciones Cardiovasculares Carlos III (CNIC), 28029 Madrid, Spain.
Menno J OudhoffCentre of Molecular Inflammation Research (CEMIR), Department of Clinical and Molecular Medicine, Faculty of Medicine and Health Sciences, Norwegian University of Science and Technology, 7491 Trondheim, Norway.
Stephen J WeissDivision of Molecular Medicine and Genetics, Department of Internal Medicine, Life Sciences Institute, University of Michigan, Ann Arbor, MI 48109, USA.
Alicia G ArroyoMatrix Metalloproteinases in Angiogenesis and Inflammation Group, Centro Nacional de Investigaciones Cardiovasculares Carlos III (CNIC), 28029 Madrid, Spain agarroyo@cnic.es.ORCID http://orcid.org/0000-0002-1536-3846
Spanish National Centre for Cardiovascular Research · ESNorwegian University of Science and Technology · NOUniversity of Michigan · US

Funding

CELLULAR AND MOLECULAR BIOLOGY AT MICHIGANT32GM007315 · NIGMS · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI PUTHENVEEDU, MANOJKUMAR A · 1985 to 2021
$12.8M
FUNCTION OF THE MEMBRANE TYPE MATRIX METALLOPROTEINASER01CA071699 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WEISS, STEPHEN J · 1997 to 2024
$7.3M
METALLOPROTEASE DEPENDENT FIBRINOLYSIS AND ANGIOGENESISR01CA088308 · NCI · UNIVERSITY OF MICHIGAN AT ANN ARBOR · PI WEISS, STEPHEN J · 2000 to 2015
$4.6M
NCI NIH HHS R01 CA071699NCI NIH HHS R01 CA088308NIGMS NIH HHS T32 GM007315
6 · The paper itself

Abstract

Cadherin-based intercellular adhesions are essential players in epithelial homeostasis, but their dynamic regulation during tissue morphogenesis and remodeling remain largely undefined. Here, we characterize an unexpected role for the membrane-anchored metalloproteinase MT2-MMP in regulating epithelial cell quiescence. Following co-immunoprecipitation and mass spectrometry, the MT2-MMP cytosolic tail was found to interact with the zonula occludens protein-1 (ZO-1) at the apical junctions of polarized epithelial cells. Functionally, MT2-MMP localizes in the apical domain of epithelial cells where it cleaves E-cadherin and promotes epithelial cell accumulation, a phenotype observed in 2D polarized cells as well as 3D cysts. MT2-MMP-mediated cleavage subsequently disrupts apical E-cadherin-mediated cell quiescence resulting in relaxed apical cortical tension favoring cell extrusion and re-sorting of Src kinase activity to junctional complexes, thereby promoting proliferation. Physiologically, MT2-MMP loss of function alters E-cadherin distribution, leading to impaired 3D organoid formation by mouse colonic epithelial cells

Indexed as

Adherens JunctionsCadherinsCell MovementCytoskeletal ProteinsEpithelial CellsHomeostasisHumansIntercellular JunctionsIntestinal MucosaMatrix Metalloproteinase 15Tight JunctionsCadherinsCytoskeletal ProteinsMatrix Metalloproteinase 15MMP15 protein, humanApical junctionE-cadherinEpithelial cell proliferationMT2-MMPSrcZO-1

Identifiers

PMID29061881
PMCPMC5769589
OpenAlexW2767040033

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.