Evidence map›Paper›PMID 30760555›Full record

ArticleLife science alliance2019

Epithelial polarization in 3D matrix requires DDR1 signaling to regulate actomyosin contractility.

Pia Pernille Søgaard, Noriko Ito, Nanami Sato, Yasuyuki Fujita, Karl Matter, Yoshifumi Itoh

Open access · goldAbstract read
PubMed Full text at PMC Publisher
In one paragraph

Article in Life science alliance, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.

0numbers the graph read from it
0cells of the map it votes in
4citing papers in PubMed
0.5field-weighted citation impact, top 37% 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

4 citing papers in PubMed, 10 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
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

6 authors at 3 institutions in 2 countries.

Pia Pernille SøgaardKennedy Institute of Rheumatology, University of Oxford, Oxford, UK.
Noriko ItoKennedy Institute of Rheumatology, University of Oxford, Oxford, UK.
Nanami SatoInstitute for Genetic Medicine, Division of Molecular Oncology, Hokkaido University, Sapporo, Japan.
Yasuyuki FujitaInstitute for Genetic Medicine, Division of Molecular Oncology, Hokkaido University, Sapporo, Japan.
Karl MatterUCL Institute of Ophthalmology, University College London, London, UK.ORCID 0000-0001-8026-7220
Yoshifumi ItohKennedy Institute of Rheumatology, University of Oxford, Oxford, UK yoshi.itoh@kennedy.ox.ac.uk.ORCID 0000-0002-2128-2823
University of Oxford · GBHokkaido University · JPUniversity College London · GB

Funding

Biotechnology and Biological Sciences Research Council BB/N014855/1
6 · The paper itself

Abstract

Epithelial cells form sheets and tubules in various epithelial organs and establish apicobasal polarity and asymmetric vesicle transport to provide functionality in these structures. However, the molecular mechanisms that allow epithelial cells to establish polarity are not clearly understood. Here, we present evidence that the kinase activity of the receptor tyrosine kinase for collagen, discoidin domain receptor 1 (DDR1), is required for efficient establishment of epithelial polarity, proper asymmetric protein secretion, and execution of morphogenic programs. Lack of DDR1 protein or inhibition of DDR1 kinase activity disturbed tubulogenesis, cystogenesis, and the establishment of epithelial polarity and caused defects in the polarized localization of membrane-type 1 matrix metalloproteinase (MT1-MMP), GP135, primary cilia, laminin, and the Golgi apparatus. Disturbed epithelial polarity and cystogenesis upon DDR1 inhibition was caused by excess ROCK (rho-associated, coiled-coil-containing protein kinase)-driven actomyosin contractility, and pharmacological inhibition of ROCK was sufficient to correct these defects. Our data indicate that a DDR1-ROCK signaling axis is essential for the efficient establishment of epithelial polarity.

Indexed as

ActomyosinAnimalsCaco-2 CellsCell PolarityCiliaContactin 1Discoidin Domain Receptor 1DogsEpithelial CellsFemaleGolgi ApparatusHumansLamininMadin Darby Canine Kidney CellsMaleMatrix Metalloproteinase 14ActomyosinContactin 1DDR1 protein, humanDdr1 protein, mouseDiscoidin Domain Receptor 1LamininMatrix Metalloproteinase 14MMP14 protein, humanMmp14 protein, mouserho-Associated Kinases

Identifiers

PMID30760555
PMCPMC6374992
OpenAlexW2912337978

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.