Evidence map›Paper›PMID 22315223›Full record

ArticleThe Journal of biological chemistry2012

Membrane type 1 matrix metalloproteinase (MT1-MMP) ubiquitination at Lys581 increases cellular invasion through type I collagen.

Patricia A Eisenach, Pedro Corrêa de Sampaio, Gillian Murphy, Christian Roghi

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed, 1 pooled it
1.4field-weighted citation impact, top 18% 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

23 citing papers in PubMed, 1 synthesis or guideline pooled it, 36 citations in OpenAlex.

  1. Pooled it
  2. Article
  3. Review
  4. Article
  5. Review
  6. Cytoplasmic Tail of MT1-MMP: A Hub of MT1-MMP Regulation and Function.International journal of molecular sciences · 2023
    Review
  7. Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. The Expanding Role of MT1-MMP in Cancer Progression.Pharmaceuticals (Basel, Switzerland) · 2019
    Review
  16. Article
  17. Article
  18. Article
  19. MMP-14 in skeletal muscle repair.Journal of muscle research and cell motility · 2015
    Review
  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

4 authors at 4 institutions in 2 countries.

Patricia A EisenachDepartment of Oncology, Cancer Research UK Cambridge Research Institute, Li Ka Shing Centre, Robinson Way, University of Cambridge, Cambridge CB2 0RE, United Kingdom. eisenach@biochem.mpg.de
Pedro Corrêa de Sampaio
Gillian Murphy
Christian Roghi
Cancer Research UK · GBCentre for Cancer Biology · AUUniversity of Cambridge · GBUniversity of East Anglia · GB

Funding

Cancer Research UK
6 · The paper itself

Abstract

Membrane type 1 matrix metalloproteinase (MT1-MMP/MMP14) is a zinc-dependent type I transmembrane metalloproteinase playing pivotal roles in the regulation of pericellular proteolysis and cellular migration. Elevated expression levels of MT1-MMP have been demonstrated to correlate with a poor prognosis in cancer. MT1-MMP has a short intracellular domain (ICD) that has been shown to play important roles in cellular migration and invasion, although these ICD-mediated mechanisms remain poorly understood. In this study, we report that MT1-MMP is mono-ubiquitinated at its unique lysine residue (Lys(581)) within the ICD. Our data suggest that this post-translational modification is involved in MT1-MMP trafficking as well as in modulating cellular invasion through type I collagen matrices. By using an MT1-MMP Y573A mutant or the Src family inhibitor PP2, we observed that the previously described Src-dependent MT1-MMP phosphorylation is a prerequisite for ubiquitination. Taken together, these findings show for the first time an additional post-translational modification of MT1-MMP that regulates its trafficking and cellular invasion, which further emphasizes the key role of the MT1-MMP ICD.

Indexed as

Cell MovementLysineUbiquitinationCell Line, TumorCollagen Type IGene Expression Regulation, EnzymologicHumansIntracellular SpaceMatrix Metalloproteinase 14Mutagenesis, Site-DirectedMutationPhosphorylationProtein Structure, TertiaryProtein TransportProteolysisProto-Oncogene Proteins pp60(c-src)Collagen Type ILysineMatrix Metalloproteinase 14Proto-Oncogene Proteins pp60(c-src)

Identifiers

PMID22315223
PMCPMC3322893
OpenAlexW2124614974

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.