Evidence map›Paper›PMID 34509508›Full record

ArticleBiophysical journal2021

Exploring the influence of cytosolic and membrane FAK activation on YAP/TAZ nuclear translocation.

Kerbaï Saïd Eroumé, Rachel Cavill, Katerina Staňková, Jan de Boer, Aurélie Carlier

Abstract read
In one paragraph

Article in Biophysical journal, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
–field-weighted citation impact
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

9 citing papers in PubMed.

  1. Article
  2. Article
  3. Article
  4. Article
  5. YAP/TAZ drives Notch and angiogenesis mechanoregulation in silico.NPJ systems biology and applications · 2024
    Article
  6. Article
  7. Review
  8. Review
  9. 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

5 authors.

Kerbaï Saïd ErouméMERLN Institute for Technology-Inspired Regenerative Medicine, Maastricht University, Maastricht, the Netherlands.
Rachel CavillDepartment of Data Science and Knowledge Engineering, Faculty of Science and Engineering, Maastricht University, Maastricht, the Netherlands.
Katerina StaňkováDepartment of Data Science and Knowledge Engineering, Faculty of Science and Engineering, Maastricht University, Maastricht, the Netherlands.
Jan de BoerDepartment of Biomedical Engineering and Institute for Complex Molecular Systems, Eindhoven University of Technology, Eindhoven, the Netherlands.
Aurélie CarlierMERLN Institute for Technology-Inspired Regenerative Medicine, Maastricht University, Maastricht, the Netherlands. Electronic address: a.carlier@maastrichtuniversity.nl.

Funding

Mechanistic Modeling of Cellular SystemsR24GM137787 · NIGMS · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI Pedro Mendes, Ion I. Moraru · 2020 to 2026
$8.9M
NIGMS NIH HHS R24 GM137787
6 · The paper itself

Abstract

Membrane binding and unbinding dynamics play a crucial role in the biological activity of several nonintegral membrane proteins, which have to be recruited to the membrane to perform their functions. By localizing to the membrane, these proteins are able to induce downstream signal amplification in their respective signaling pathways. Here, we present a 3D computational approach using reaction-diffusion equations to investigate the relation between membrane localization of focal adhesion kinase (FAK), Ras homolog family member A (RhoA), and signal amplification of the YAP/TAZ signaling pathway. Our results show that the theoretical scenarios in which FAK is membrane bound yield robust and amplified YAP/TAZ nuclear translocation signals. Moreover, we predict that the amount of YAP/TAZ nuclear translocation increases with cell spreading, confirming the experimental findings in the literature. In summary, our in silico predictions show that when the cell membrane interaction area with the underlying substrate increases, for example, through cell spreading, this leads to more encounters between membrane-bound signaling partners and downstream signal amplification. Because membrane activation is a motif common to many signaling pathways, this study has important implications for understanding the design principles of signaling networks.

Indexed as

Adaptor Proteins, Signal TransducingTranscription FactorsFocal Adhesion Protein-Tyrosine KinasesPhosphoproteinsSignal TransductionTrans-ActivatorsAdaptor Proteins, Signal TransducingFocal Adhesion Protein-Tyrosine KinasesPhosphoproteinsTrans-ActivatorsTranscription Factors

Identifiers

PMID34509508
PMCPMC8553670

What OpenQuestion holds

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Registered trials

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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.