MassIVE MSV000093379

Partial Public PXD046896

Leiomodin 1 promotes myogenic differentiation by modulating Sirtuin 1 localization

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Description

During myogenesis, the cell architecture and thereby the proteome undergoes extensive remodelling to enable muscle development and regeneration, a process which is only partially characterised and understood and displays impairments in age and disease. By analysing the protein expression dynamics during myogenic differentiation using mass spectrometry we identified the actin nucleator protein leiomodin 1 (LMOD1) among a subset of proteins that increase abundance in early phases of myogenesis. Knockdown of Lmod1 in primary myoblasts severely affected the terminal differentiation and fusion of myotubes. We show that LMOD1 interacts with the deacetylase sirtuin 1 (SIRT1) and that depletion or pharmacological inhibition of SIRT1 partially rescues the effects of Lmod1 knockdown. Both LMOD1 and SIRT1 re-distribute from the nucleus to cytoplasm during myogenic differentiation and their localization correlates especially at the onset of myogenic differentiation. We show that overexpression of LMOD1 is sufficient to alter SIRT1 localization, de-repress SIRT1 target genes, promote accelerated myotube formation and improve myoblast fusion. Our work identifies a novel regulator of myogenesis that might be targeted to improve muscle regeneration in aging and disease. [doi:10.25345/C5N010450] [dataset license: CC0 1.0 Universal (CC0 1.0)]

Keywords: muscle stem cells, MuSCs, cytoskeleton dynamics, myogenesis, Lmod1, Sirt1, mass spectrometry, differentiation

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Principal Investigators:
(in alphabetical order) 		Alessandro Ori, Leibniz Institute on Aging Fritz Lipmann Institute (FLI), Germany
Submitting User: ProteomicsCF_FLI
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