Evidence map›Paper›PMID 26240176›Full record

ArticleJournal of cell science2015

Vinculin phosphorylation at residues Y100 and Y1065 is required for cellular force transmission.

Vera Auernheimer, Lena A Lautscham, Maria Leidenberger, Oliver Friedrich, Barbara Kappes, Ben Fabry, Wolfgang H Goldmann

Open access · bronzeAbstract read
In one paragraph

Article in Journal of cell science, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 38 papers.

0numbers the graph read from it
0cells of the map it votes in
38citing papers in PubMed
3.6field-weighted citation impact, top 7% 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

38 citing papers in PubMed, 65 citations in OpenAlex.

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  15. Article
  16. Article
  17. Manipulation of Focal Adhesion Signaling by Pathogenic Microbes.International journal of molecular sciences · 2021
    Review
  18. Article
  19. Article
  20. Molecular Tension Sensors: Moving Beyond Force.Current opinion in biomedical engineering · 2019
    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

7 authors at 1 institution in 1 country.

Vera AuernheimerDepartment of Physics, Biophysics Group, University of Erlangen-Nuremberg, 91052 Erlangen, Germany.
Lena A LautschamDepartment of Physics, Biophysics Group, University of Erlangen-Nuremberg, 91052 Erlangen, Germany.
Maria LeidenbergerInstitute of Medical Biotechnology, Department of Chemical and Biological Engineering University of Erlangen-Nuremberg, 91052 Erlangen, Germany.
Oliver FriedrichInstitute of Medical Biotechnology, Department of Chemical and Biological Engineering University of Erlangen-Nuremberg, 91052 Erlangen, Germany.
Barbara KappesInstitute of Medical Biotechnology, Department of Chemical and Biological Engineering University of Erlangen-Nuremberg, 91052 Erlangen, Germany.
Ben FabryDepartment of Physics, Biophysics Group, University of Erlangen-Nuremberg, 91052 Erlangen, Germany.
Wolfgang H GoldmannDepartment of Physics, Biophysics Group, University of Erlangen-Nuremberg, 91052 Erlangen, Germany wgoldmann@biomed.uni-erlangen.de.
Friedrich-Alexander-Universität Erlangen-Nürnberg · DE

Funding

Micromechanics of the airway smooth muscle cellR01HL065960 · NHLBI · HARVARD UNIVERSITY (SCH OF PUBLIC HLTH) · PI FREDBERG, JEFFREY J · 2000 to 2009
$6.3M
NHLBI NIH HHS HL65960NHLBI NIH HHS R01 HL065960
6 · The paper itself

Abstract

The focal adhesion protein vinculin connects the actin cytoskeleton, through talin and integrins, with the extracellular matrix. Vinculin consists of a globular head and tail domain, which undergo conformational changes from a closed auto-inhibited conformation in the cytoplasm to an open conformation in focal adhesions. Src-mediated phosphorylation has been suggested to regulate this conformational switch. To explore the role of phosphorylation in vinculin activation, we used knock-out mouse embryonic fibroblasts re-expressing different vinculin mutants in traction microscopy, magnetic tweezer microrheology, FRAP and actin-binding assays. Compared to cells expressing wild-type or constitutively active vinculin, we found reduced tractions, cytoskeletal stiffness, adhesion strength, and increased vinculin dynamics in cells expressing constitutively inactive vinculin or vinculin where Src-mediated phosphorylation was blocked by replacing tyrosine at position 100 and/or 1065 with a non-phosphorylatable phenylalanine residue. Replacing tyrosine residues with phospho-mimicking glutamic acid residues restored cellular tractions, stiffness and adhesion strength, as well as vinculin dynamics, and facilitated vinculin-actin binding. These data demonstrate that Src-mediated phosphorylation is necessary for vinculin activation, and that phosphorylation controls cytoskeletal mechanics by regulating force transmission between the actin cytoskeleton and focal adhesion proteins.

Indexed as

AnimalsCell AdhesionCytoskeletonEnergy TransferFibroblastsIntegrinsMiceMice, KnockoutPhosphorylationPoint MutationProtein Structure, Secondarysrc-Family KinasesVinculinIntegrinssrc-Family KinasesVinculinActin pulldownCell stiffnessFocal adhesionFRAPMechanotransductionTractionTyrosine phosphorylationVinculin

Identifiers

PMID26240176
PMCPMC4582403
OpenAlexW2322970665

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.