Evidence map›Paper›PMID 25918420›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2015

Inverted formin 2 in focal adhesions promotes dorsal stress fiber and fibrillar adhesion formation to drive extracellular matrix assembly.

Colleen T Skau, Sergey V Plotnikov, Andrew D Doyle, Clare M Waterman

RetractedOpen access · bronzeAbstract readRetracted Publication
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. It has been retracted, and should not be counted. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
4.7field-weighted citation impact, top 5% 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

22 citing papers in PubMed, 37 citations in OpenAlex.

  1. Article
  2. Ultrastructure of the actin cytoskeleton.Current opinion in cell biology · 2018
    Review
  3. Review
  4. Article
  5. Article
  6. Inverted formins: A subfamily of atypical formins.Cytoskeleton (Hoboken, N.J.) · 2017
    Review
  7. Article
  8. Article
  9. Review
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Article
  18. Review
  19. Article
  20. Review
4 · The record

Corrections and comments

5 · Who and what money

Authors and funding

4 authors at 3 institutions in 2 countries.

Colleen T SkauCell Biology and Physiology Center, National Heart Lung and Blood Institute, and.
Sergey V PlotnikovDepartment of Cell and Systems Biology, University of Toronto, Toronto, ON, Canada M5S 3G5.
Andrew D DoyleCell Biology Section, Laboratory of Cell and Developmental Biology, National Institute of Dental and Craniofacial Research, NIH, Bethesda, MD 20892; and.
Clare M WatermanCell Biology and Physiology Center, National Heart Lung and Blood Institute, and watermancm@nhlbi.nih.gov.
National Heart Lung and Blood Institute · USNational Institute of Dental and Craniofacial Research · USUniversity of Toronto · CA

Funding

Integration of Actin Dynamics and Adhesion in Cell MigrationZIAHL005105 · NHLBI · NATIONAL HEART, LUNG, AND BLOOD INSTITUTE · PI WATERMAN, CLARE MICHAL · 2009 to 2025
$16.5M
Intramural NIH HHS
6 · The paper itself

Abstract

Actin filaments and integrin-based focal adhesions (FAs) form integrated systems that mediate dynamic cell interactions with their environment or other cells during migration, the immune response, and tissue morphogenesis. How adhesion-associated actin structures obtain their functional specificity is unclear. Here we show that the formin-family actin nucleator, inverted formin 2 (INF2), localizes specifically to FAs and dorsal stress fibers (SFs) in fibroblasts. High-resolution fluorescence microscopy and manipulation of INF2 levels in cells indicate that INF2 plays a critical role at the SF-FA junction by promoting actin polymerization via free barbed end generation and centripetal elongation of an FA-associated actin bundle to form dorsal SF. INF2 assembles into FAs during maturation rather than during their initial generation, and once there, acts to promote rapid FA elongation and maturation into tensin-containing fibrillar FAs in the cell center. We show that INF2 is required for fibroblasts to organize fibronectin into matrix fibers and ultimately 3D matrices. Collectively our results indicate an important role for the formin INF2 in specifying the function of fibrillar FAs through its ability to generate dorsal SFs. Thus, dorsal SFs and fibrillar FAs form a specific class of integrated adhesion-associated actin structure in fibroblasts that mediates generation and remodeling of ECM.

Indexed as

ActinsAnimalsCell AdhesionCytoskeletonExtracellular MatrixFibroblastsFibronectinsFocal AdhesionsForminsGreen Fluorescent ProteinsHumansIntegrinsMiceMicrofilament ProteinsMicroscopy, ConfocalMicroscopy, FluorescenceActinsFibronectinsForminsGreen Fluorescent ProteinsINF2 protein, humanINF2 protein, mouseIntegrinsMicrofilament ProteinsProtein IsoformsRNA, Small Interferingactinfluorescence microscopyINF2integrin

Identifiers

PMID25918420
PMCPMC4434736
OpenAlexW1993602817

What OpenQuestion holds

Textmetadata
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.