Evidence map›Paper›PMID 27353427›Full record

ArticleScientific reports2016

The actin crosslinking protein palladin modulates force generation and mechanosensitivity of tumor associated fibroblasts.

Mikheil Azatov, Silvia M Goicoechea, Carol A Otey, Arpita Upadhyaya

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
2.7field-weighted citation impact, top 11% 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

15 citing papers in PubMed, 23 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Review
  6. Article
  7. Article
  8. Review
  9. Review
  10. Article
  11. Article
  12. The Role of Palladin in Podocytes.Journal of the American Society of Nephrology : JASN · 2018
    Article
  13. Article
  14. Article
  15. Traction Force Microscopy for Noninvasive Imaging of Cell Forces.Advances in experimental medicine and biology
    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

4 authors at 3 institutions in 1 country.

Mikheil AzatovDepartment of Physics, University of Maryland, College Park MD 20742, USA.
Silvia M GoicoecheaDepartment of Biological Sciences, University of Toledo, Toledo, Ohio, 43606, USA.
Carol A OteyDepartment of Cell Biology and Physiology and the Lineberger Comprehensive Cancer Center, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.
Arpita UpadhyayaDepartment of Physics, University of Maryland, College Park MD 20742, USA.
University of Maryland, College Park · USUniversity of North Carolina at Chapel Hill · USUniversity of Toledo · US

Funding

Virology Research Program (Program 4)P30CA016086 · NCI · UNIV OF NORTH CAROLINA CHAPEL HILL · PI Deborah F. Tate · 1985 to 2026
$201.5M
NCI NIH HHS P30 CA016086
6 · The paper itself

Abstract

Cells organize actin filaments into higher-order structures by regulating the composition, distribution and concentration of actin crosslinkers. Palladin is an actin crosslinker found in the lamellar actin network and stress fibers, which are critical for mechanosensing of the environment. Palladin also serves as a molecular scaffold for α-actinin, another key actin crosslinker. By virtue of its close interactions with actomyosin structures in the cell, palladin may play an important role in cell mechanics. However, the role of palladin in cellular force generation and mechanosensing has not been studied. Here, we investigate the role of palladin in regulating the plasticity of the actin cytoskeleton and cellular force generation in response to alterations in substrate stiffness. Traction force microscopy revealed that tumor-associated fibroblasts generate larger forces on substrates of increased stiffness. Contrary to expectations, knocking down palladin increased the forces generated by cells and inhibited their ability to sense substrate stiffness for very stiff gels. This was accompanied by significant differences in actin organization, adhesion dynamics and altered myosin organization in palladin knock-down cells. Our results suggest that actin crosslinkers such as palladin and myosin motors coordinate for optimal cell function and to prevent aberrant behavior as in cancer metastasis.

Indexed as

ActinsCancer-Associated FibroblastsCell AdhesionCells, CulturedCytoskeletal ProteinsFocal AdhesionsHeterocyclic Compounds, 4 or More RingsHumansMechanotransduction, CellularPhosphoproteinsActinsblebbistatinCytoskeletal ProteinsHeterocyclic Compounds, 4 or More RingsPALLD protein, humanPhosphoproteins

Identifiers

PMID27353427
PMCPMC4926206
OpenAlexW2463369896

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.