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Solagna, F.* ; Nogara, L.* ; Dyar, K.A. ; Greulich, F.* ; Mir, A.A. ; Türk, C.* ; Bock, T.* ; Geremia, A.* ; Baraldo, M.* ; Sartori, R.* ; Farup, J.* ; Uhlenhaut, N.H. ; Vissing, K.* ; Krüger, M.* ; Blaauw, B.*

Exercise-dependent increases in protein synthesis are accompanied by chromatin modifications and increased MRTF-SRF signalling.

Acta Physiol. 230:e13496 (2020)
Verlagsversion Postprint Forschungsdaten DOI
Open Access Gold (Paid Option)
Creative Commons Lizenzvertrag
Aim Resistance exercise increases muscle mass over time. However, the early signalling events leading to muscle growth are not yet well-defined. Here, we aim to identify new signalling pathways important for muscle remodelling after exercise.Methods We performed a phosphoproteomics screen after a single bout of exercise in mice. As an exercise model we used unilateral electrical stimulation in vivo and treadmill running. We analysed muscle biopsies from human subjects to verify if our findings in murine muscle also translate to exercise in humans.Results We identified a new phosphorylation site on Myocardin-Related Transcription Factor B (MRTF-B), a co-activator of serum response factor (SRF). Phosphorylation of MRTF-B is required for its nuclear translocation after exercise and is accompanied by the transcription of the SRF target gene Fos. In addition, high-intensity exercise also remodels chromatin at specific SRF target gene loci through the phosphorylation of histone 3 on serine 10 in myonuclei of both mice and humans. Ablation of the MAP kinase member MSK1/2 is sufficient to prevent this histone phosphorylation, reduce induction of SRF-target genes, and prevent increases in protein synthesis after exercise.Conclusion Our results identify a new exercise signalling fingerprint in vivo, instrumental for exercise-induced protein synthesis and potentially muscle growth.
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Publikationstyp Artikel: Journalartikel
Dokumenttyp Wissenschaftlicher Artikel
Schlagwörter Exercise ; Histone Phosphorylation ; Protein Synthesis ; Serum Response Factor ; Skeletal Muscle; Human Skeletal-muscle; Actin Dynamics; In-vivo; Phosphorylation; Transcription; Platform; Stars; Transduction; Mechanism; Pathway
ISSN (print) / ISBN 1748-1708
e-ISSN 1748-1716
Zeitschrift Acta Physiologica
Quellenangaben Band: 230, Heft: 1, Seiten: , Artikelnummer: e13496 Supplement: ,
Verlag Wiley
Verlagsort Hoboken
Begutachtungsstatus Peer reviewed