Evidence map›Paper›PMID 22792288›Full record

ArticlePloS one2012

Loss of the integrin-activating transmembrane protein Fam38A (Piezo1) promotes a switch to a reduced integrin-dependent mode of cell migration.

Brian J McHugh, Amanda Murdoch, Christopher Haslett, Tariq Sethi

Open access · goldAbstract read
In one paragraph

Article in PloS one, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 94 papers.

0numbers the graph read from it
0cells of the map it votes in
94citing papers in PubMed
2.7field-weighted citation impact, top 10% 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

94 citing papers in PubMed, 166 citations in OpenAlex.

  1. Stretch-activated ion channel Piezo1 directs lineage choice in human neural stem cells.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Trial
  2. Review
  3. Cancer pain.Nature reviews. Disease primers · 2026
    Review
  4. Review
  5. Review
  6. Article
  7. Review
  8. Review
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Piezo1 ion channels are capable of conformational signaling.bioRxiv : the preprint server for biology · 2024
    Article
  15. Article
  16. Article
  17. Review
  18. The mechanism and potential therapeutic target of piezo channels in pain.Frontiers in pain research (Lausanne, Switzerland) · 2024
    Review
  19. Review
  20. Article

34 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Brian J McHughMedical Research Council Centre for Inflammation Research, University of Edinburgh, Edinburgh, Midlothian, United Kingdom. Brian.McHugh@ed.ac.uk
Amanda Murdoch
Christopher Haslett
Tariq Sethi
Medical Research Council · GBKing's College London · GBUniversity of Edinburgh · GB

Funding

Chief Scientist Office CZB/4/691Medical Research Council G0901697
6 · The paper itself

Abstract

Lung cancer is one of the most common fatal diseases in the developed world. The disease is rarely cured by currently available therapies, with an overall survival rate of ∼10%. Characterizing novel proteins that offer crucial insights into the processes of lung tumour invasion and metastasis may therefore provide much-needed prognostic markers, and influence therapeutic strategies. Aberrant function of the integrin family of heterodimeric cell surface receptors is a common theme in cancer--investigation into novel integrin activity regulators may offer crucial insights into the processes of tumour invasion and metastasis and may reveal insights into potential therapeutic targets. We previously described that depletion of the novel multi-transmembrane domain protein Fam38A, located at the endoplasmic reticulum (ER), inactivates endogenous beta1 integrin affinity, reducing cell adhesion. We now show that depletion of Fam38A, also now known as Piezo1, causes anchorage independence and a switch to a reduced integrin-dependent mode of cell migration/invasion, a novel phenotype for this integrin-regulating protein. Normal lung epithelial cells show increased rates of migration by 2D time-lapse microscopy and increased capacity to invade into matrigel, despite having decreased integrin affinity. We confirm greatly depleted Fam38A expression in small cell lung cancer (SCLC) lines where a form of reduced integrin-dependent migration, i.e. amoeboid migration, is a known phenotype. We propose that loss of Fam38A expression may cause increased cell migration and metastasis in lung tumours.

Indexed as

Cell MovementActin CytoskeletonCalpainCell AdhesionCell Line, TumorGene ExpressionGene Knockdown TechniquesHumansIntegrinsIon ChannelsLoss of HeterozygosityLung NeoplasmsMicrofilament ProteinsRNA, Small InterferingSmall Cell Lung CarcinomaTensinsCalpainIntegrinsIon ChannelsMicrofilament ProteinsPIEZO1 protein, humanRNA, Small InterferingTensins

Identifiers

PMID22792288
PMCPMC3390408
OpenAlexW1995062036

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.