Evidence map›Paper›PMID 27068537›Full record

ArticleJournal of cell science2016

Nuclear transport of paxillin depends on focal adhesion dynamics and FAT domains.

Aneesh R Sathe, G V Shivashankar, Michael P Sheetz

Open access · hybridAbstract read
In one paragraph

Article in Journal of cell science, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.

0numbers the graph read from it
0cells of the map it votes in
16citing papers in PubMed
3.2field-weighted citation impact, top 9% 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

16 citing papers in PubMed, 35 citations in OpenAlex.

  1. Review
  2. Review
  3. Article
  4. Review
  5. Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021
    Review
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. Why the impact of mechanical stimuli on stem cells remains a challenge.Cellular and molecular life sciences : CMLS · 2018
    Review
  12. Review
  13. Review
  14. Article
  15. Review
  16. Focal adhesion kinase signaling in unexpected places.Current opinion in cell biology · 2017
    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

3 authors at 2 institutions in 3 countries.

Aneesh R SatheMechanobiology Institute, National University of Singapore, Singapore 117411.
G V ShivashankarMechanobiology Institute, National University of Singapore, Singapore 117411 Department of Biological Sciences, National University of Singapore, Singapore 117543 IFOM-NUS Joint Research Laboratory.
Michael P SheetzMechanobiology Institute, National University of Singapore, Singapore 117411 IFOM-NUS Joint Research Laboratory Department of Biological Sciences, Columbia University, New York, NY 10027, USA ms2001@columbia.edu.
National University of Singapore · SGColumbia University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The nuclear transport of paxillin appears to be crucial for paxillin function but the mechanism of transport remains unclear. Here, we show that the nuclear transport of paxillin is regulated by focal adhesion turnover and the presence of FAT domains. Focal adhesion turnover was controlled using triangular or circular fibronectin islands. Circular islands caused higher focal adhesion turnover and increased the nuclear transport of paxillin relative to triangular islands. Mutating several residues of paxillin had no effect on its nuclear transport, suggesting that the process is controlled by multiple domains. Knocking out FAK (also known as PTK2) and vinculin caused an increase in nuclear paxillin. This could be reversed by rescue with wild-type FAK but not by FAK with a mutated FAT domain, which inhibits paxillin binding. Expressing just the FAT domain of FAK not only brought down nuclear levels of paxillin but also caused a large immobile fraction of paxillin to be present at focal adhesions, as demonstrated by fluorescence recovery after photobleaching (FRAP) studies. Taken together, focal adhesion turnover and FAT domains regulate the nuclear localization of paxillin, suggesting a possible role for transcriptional control, through paxillin, by focal adhesions.

Indexed as

Active Transport, Cell NucleusCell AdhesionFibroblastsFibronectinsFocal Adhesion Kinase 1Focal AdhesionsGene Knockout TechniquesHumansPaxillinProtein BindingProtein DomainsVinculinFibronectinsFocal Adhesion Kinase 1PaxillinPTK2 protein, humanVinculinFAT domainFocal adhesionNucleusPaxillin

Identifiers

PMID27068537
PMCPMC4895192
OpenAlexW2319356944

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.