Evidence map›Paper›PMID 19294408›Full record

ArticleEuropean journal of applied physiology2009

Mechano-transduction to muscle protein synthesis is modulated by FAK.

Stephan Klossner, Anne-Cecile Durieux, Damien Freyssenet, Martin Flueck

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In one paragraph

Article in European journal of applied physiology, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.

0numbers the graph read from it
0cells of the map it votes in
60citing papers in PubMed
3.1field-weighted citation impact, top 8% 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

60 citing papers in PubMed, 125 citations in OpenAlex.

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  11. CCN2 participates in overload-induced skeletal muscle hypertrophy.Matrix biology : journal of the International Society for Matrix Biology · 2022
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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

4 authors at 3 institutions in 3 countries.

Stephan KlossnerInstitute of Anatomy, University of Berne, Berne, Switzerland.
Anne-Cecile Durieux
Damien Freyssenet
Martin Flueck
University of Bern · CHManchester Metropolitan University · GBUniversité Jean Monnet · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We examined the involvement of focal adhesion kinase (FAK) in mechano-regulated signalling to protein synthesis by combining muscle-targeted transgenesis with a physiological model for un- and reloading of hindlimbs. Transfections of mouse tibialis anterior muscle with a FAK expression construct increased FAK protein 1.6-fold versus empty transfection in the contralateral leg and elevated FAK concentration at the sarcolemma. Altered activation status of phosphotransfer enzymes and downstream translation factors showed that FAK overexpression was functionally important. FAK auto-phosphorylation on Y397 was enhanced between 1 and 6 h of reloading and preceded the activation of p70S6K after 24 h of reloading. Akt and translation initiation factors 4E-BP1 and 2A, which reside up- or downstream of p70S6K, respectively, showed no FAK-modulated regulation. The findings identify FAK as an upstream element of the mechano-sensory pathway of p70S6K activation whose Akt-independent regulation intervenes in control of muscle mass by mechanical stimuli in humans.

Indexed as

AnimalsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesMaleMechanotransduction, CellularMiceMitogen-Activated Protein Kinase 3Muscle ProteinsNF-kappa BPhosphorylationRibosomal Protein S6 Kinases, 70-kDaSignal TransductionFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesMitogen-Activated Protein Kinase 3Muscle ProteinsNF-kappa BRibosomal Protein S6 Kinases, 70-kDa

Identifiers

PMID19294408
OpenAlexW2023087041

What Socratic 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 Socratic graph.