Evidence map›Paper›PMID 24989798›Full record

ArticleMolecular biology of the cell2014

Actin-associated protein palladin promotes tumor cell invasion by linking extracellular matrix degradation to cell cytoskeleton.

Pernilla von Nandelstadh, Erika Gucciardo, Jouko Lohi, Rui Li, Nami Sugiyama, Olli Carpen, Kaisa Lehti

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 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
2.1field-weighted citation impact, top 13% 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

32 citing papers in PubMed, 51 citations in OpenAlex.

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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 2 institutions in 1 country.

Pernilla von NandelstadhResearch Programs Unit, Genome-Scale Biology, Biomedicum Helsinki, University of Helsinki, Helsinki, Finland Department of Pathology, Haartman Institute, FIN-00014, University of Helsinki, Helsinki, Finland.
Erika GucciardoResearch Programs Unit, Genome-Scale Biology, Biomedicum Helsinki, University of Helsinki, Helsinki, Finland Department of Pathology, Haartman Institute, FIN-00014, University of Helsinki, Helsinki, Finland.
Jouko LohiDepartment of Pathology, Haartman Institute, FIN-00014, University of Helsinki, Helsinki, Finland Department of Pathology, HUSLAB, Helsinki University Central Hospital, FIN-00290, Helsinki, Finland.
Rui LiResearch Programs Unit, Genome-Scale Biology, Biomedicum Helsinki, University of Helsinki, Helsinki, Finland Department of Pathology, Haartman Institute, FIN-00014, University of Helsinki, Helsinki, Finland.
Nami SugiyamaResearch Programs Unit, Genome-Scale Biology, Biomedicum Helsinki, University of Helsinki, Helsinki, Finland Department of Pathology, Haartman Institute, FIN-00014, University of Helsinki, Helsinki, Finland.
Olli CarpenDepartment of Pathology, University of Turku and Turku University Central Hospital, FIN-20520, Turku, Finland.
Kaisa LehtiResearch Programs Unit, Genome-Scale Biology, Biomedicum Helsinki, University of Helsinki, Helsinki, Finland Department of Pathology, Haartman Institute, FIN-00014, University of Helsinki, Helsinki, Finland kaisa.lehti@helsinki.fi.
University of Helsinki · FIUniversity of Turku · FI

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Basal-like breast carcinomas, characterized by unfavorable prognosis and frequent metastases, are associated with epithelial-to-mesenchymal transition. During this process, cancer cells undergo cytoskeletal reorganization and up-regulate membrane-type 1 matrix metalloproteinase (MT1-MMP; MMP14), which functions in actin-based pseudopods to drive invasion by extracellular matrix degradation. However, the mechanisms that couple matrix proteolysis to the actin cytoskeleton in cell invasion have remained unclear. On the basis of a yeast two-hybrid screen for the MT1-MMP cytoplasmic tail-binding proteins, we identify here a novel Src-regulated protein interaction between the dynamic cytoskeletal scaffold protein palladin and MT1-MMP. These proteins were coexpressed in invasive human basal-like breast carcinomas and corresponding cell lines, where they were associated in the same matrix contacting and degrading membrane complexes. The silencing and overexpression of the 90-kDa palladin isoform revealed the functional importance of the interaction with MT1-MMP in pericellular matrix degradation and mesenchymal tumor cell invasion, whereas in MT1-MMP-negative cells, palladin overexpression was insufficient for invasion. Moreover, this invasion was inhibited in a dominant-negative manner by an immunoglobulin domain-containing palladin fragment lacking the dynamic scaffold and Src-binding domains. These results identify a novel protein interaction that links matrix degradation to cytoskeletal dynamics and migration signaling in mesenchymal cell invasion.

Indexed as

Neoplasm InvasivenessActinsBreast NeoplasmsCarcinomaCell Line, TumorConnectinCytoskeletal ProteinsCytoskeletonEpithelial-Mesenchymal TransitionExtracellular MatrixFemaleHumansMatrix Metalloproteinase 14Microfilament ProteinsPhosphoproteinsProtein IsoformsActinsConnectinCytoskeletal ProteinsMatrix Metalloproteinase 14Microfilament ProteinsMYOT protein, humanPALLD protein, humanPhosphoproteinsProtein Isoforms

Identifiers

PMID24989798
PMCPMC4148246
OpenAlexW2156542078

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.