Evidence map›Paper›PMID 26544178›Full record

ArticlePLoS computational biology2015

Mechanism of Focal Adhesion Kinase Mechanosensing.

Jing Zhou, Camilo Aponte-Santamaría, Sebastian Sturm, Jakob Tómas Bullerjahn, Agnieszka Bronowska, Frauke Gräter

Open access · goldAbstract read
In one paragraph

Article in PLoS computational biology, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 80 papers.

0numbers the graph read from it
0cells of the map it votes in
80citing papers in PubMed
5.7field-weighted citation impact, top 3% 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

80 citing papers in PubMed, 128 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Review
  9. Review
  10. Principles and regulation of mechanosensing.Journal of cell science · 2024
    Review
  11. Article
  12. Article
  13. Review
  14. Review
  15. A Hierarchical Mechanotransduction System: From Macro to Micro.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2024
    Review
  16. Review
  17. Article
  18. Article
  19. Allosteric activation of vinculin by talin.Nature communications · 2023
    Article
  20. Article

20 more citing papers are in PubMed but not listed here.

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 3 institutions in 1 country.

Jing ZhouHeidelberg Institute for Theoretical Studies, Heidelberg, Germany.
Camilo Aponte-SantamaríaHeidelberg Institute for Theoretical Studies, Heidelberg, Germany.
Sebastian SturmLeipzig University, Institute for Theoretical Physics, Leipzig, Germany.
Jakob Tómas BullerjahnLeipzig University, Institute for Theoretical Physics, Leipzig, Germany.
Agnieszka BronowskaHeidelberg Institute for Theoretical Studies, Heidelberg, Germany.
Frauke GräterHeidelberg Institute for Theoretical Studies, Heidelberg, Germany.
Heidelberg Institute for Theoretical Studies · DELeipzig University · DEHeidelberg University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Mechanosensing at focal adhesions regulates vital cellular processes. Here, we present results from molecular dynamics (MD) and mechano-biochemical network simulations that suggest a direct role of Focal Adhesion Kinase (FAK) as a mechano-sensor. Tensile forces, propagating from the membrane through the PIP2 binding site of the FERM domain and from the cytoskeleton-anchored FAT domain, activate FAK by unlocking its central phosphorylation site (Tyr576/577) from the autoinhibitory FERM domain. Varying loading rates, pulling directions, and membrane PIP2 concentrations corroborate the specific opening of the FERM-kinase domain interface, due to its remarkably lower mechanical stability compared to the individual alpha-helical domains and the PIP2-FERM link. Analyzing downstream signaling networks provides further evidence for an intrinsic mechano-signaling role of FAK in broadcasting force signals through Ras to the nucleus. This distinguishes FAK from hitherto identified focal adhesion mechano-responsive molecules, allowing a new interpretation of cell stretching experiments.

Indexed as

Models, BiologicalComputational BiologyCytoskeletal ProteinsCytoskeletonFocal Adhesion Protein-Tyrosine KinasesFocal AdhesionsMechanotransduction, CellularMembrane ProteinsMolecular Dynamics SimulationCytoskeletal ProteinsFocal Adhesion Protein-Tyrosine KinasesMembrane Proteins

Identifiers

PMID26544178
PMCPMC4636223
OpenAlexW2140542478

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.