Evidence map›Paper›PMID 23454549›Full record

ArticleExperimental cell research2013

α-actinin1 and 4 tyrosine phosphorylation is critical for stress fiber establishment, maintenance and focal adhesion maturation.

Yunfeng Feng, Hai Ngu, Shannon K Alford, Michael Ward, Frank Yin, Gregory D Longmore

Abstract read
In one paragraph

Article in Experimental cell research, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.3field-weighted citation impact, top 22% 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

24 citing papers in PubMed, 34 citations in OpenAlex.

  1. Article
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  5. Article
  6. Review
  7. Protein tyrosine phosphatase 1B is a regulator of alpha-actinin4 in the glomerular podocyte.Biochimica et biophysica acta. Molecular cell research · 2024
    Article
  8. Article
  9. Review
  10. Article
  11. Article
  12. Article
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  15. Article
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  17. Article
  18. Article
  19. α-Actinin-4 promotes metastasis in gastric cancer.Laboratory investigation; a journal of technical methods and pathology · 2017
    Article
  20. Neuronal migration is mediated by inositol hexakisphosphate kinase 1 via α-actinin and focal adhesion kinase.Proceedings of the National Academy of Sciences of the United States of America · 2017
    Article
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 1 institution in 1 country.

Yunfeng FengDepartments of Medicine, Washington University, St. Louis, MO 63110, USA. yfeng@dom.wustl.edu
Hai Ngu
Shannon K Alford
Michael Ward
Frank Yin
Gregory D Longmore
Washington University in St. Louis · US

Funding

TRANS NETWORK PROJECTSU54CA143868 · NCI · JOHNS HOPKINS UNIVERSITY · PI SEARSON, PETER C · 2009 to 2013
$13.7M
THE ROLE OF AJUBA LIM PROTEIN IN EPITHELIA BIOGENESISR01GM080673 · NIGMS · WASHINGTON UNIVERSITY · PI LONGMORE, GREGORY D. · 2007 to 2014
$2.4M
The Role of LIM Proteins in Cell Migration and AdhesionR01CA085839 · NCI · WASHINGTON UNIVERSITY · PI LONGMORE, GREGORY D. · 2000 to 2009
$2.2M
NCI NIH HHS CA143868NCI NIH HHS CA85839NCI NIH HHS R01 CA085839NCI NIH HHS U54 CA143868NIGMS NIH HHS R01 GM080673
6 · The paper itself

Abstract

In polarized, migrating cells, stress fibers are a highly dynamic network of contractile acto-myosin structures composed of bundles of actin filaments held together by actin cross-linking proteins such as α-actinins. As such, α-actinins influence actin cytoskeleton organization and dynamics and focal adhesion maturation. In response to environmental signals, α-actinins are tyrosine phosphorylated and this affects their binding to actin stress fibers; however, the cellular role of α-actinin tyrosine phosphorylation remains largely unknown. We found that non-muscle α-actinin1/4 are critical for the establishment of dorsal stress fibers and maintenance of transverse arc stress fibers. Analysis of cells genetically depleted of α-actinin1 and 4 reveals two distinct modes for focal adhesion maturation. An α-actinin1 or 4 dependent mode that uses dorsal stress fiber precursors as a template for establishing focal adhesions and their maturation, and an α-actinin-independent manner that uses transverse arc precursors to establish focal adhesions at both ends. Focal adhesions formed in the absence of α-actinins are delayed in their maturation, exhibit altered morphology, have decreased amounts of Zyxin and VASP, and reduced adhesiveness to extracellular matrix. Further rescue experiments demonstrate that the tyrosine phosphorylation of α-actinin1 at Y12 and α-actinin4 at Y265 is critical for dorsal stress fiber establishment, transverse arc maintenance and focal adhesion maturation.

Indexed as

ActininCell AdhesionCell Adhesion MoleculesCell DifferentiationCell Line, TumorFocal Adhesion Kinase 1Focal AdhesionsHEK293 CellsHumansMicrofilament ProteinsPaxillinPhosphoproteinsPhosphorylationProtein-Tyrosine KinasesStress FibersTyrosineActininACTN1 protein, humanACTN4 protein, humanCell Adhesion MoleculesFocal Adhesion Kinase 1Microfilament ProteinsPaxillinPhosphoproteinsProtein-Tyrosine KinasesPTK2 protein, humanPXN protein, humanTyrosineVasodilator-Stimulated PhosphoproteinZyxinZYX protein, human

Identifiers

PMID23454549
PMCPMC4142059
OpenAlexW2021996775

What OpenQuestion holds

Textmetadata
LicenceTDM
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.