Dataset Information


C-terminal FLNc in vivo kinase assay

ABSTRACT: The Z-disc is a protein-rich structure critically important for myofibril development and integrity. Since a role of the Z-disc for signal integration and transduction was recently suggested, its precise phosphorylation landscape warranted in-depth analysis. We therefore established a site-resolved protein phosphorylation map of the Z-disc in skeletal myocytes and found that it is a phosphorylation hotspot in living cells, underscoring its functions in signalling and disease-related processes. In an exemplary fashion, we analysed the actin-binding multi-adaptor protein filamin C (FLNc), which is essential for Z-disc assembly and maintenance, and found that PKC phosphorylation at distinct serine residues in its hinge 2 region prevents its cleavage at an adjacent tyrosine residue by calpain 1. With this quantitative in vivo kinase assay, we show that the phosphorylation site S2625 in mouse FLNc is significantly down-regulated upon treatment of C2C12 myotubes with the PKCα inhibitor Gö6976.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Mus Musculus (mouse)

SUBMITTER: Friedel Drepper  

LAB HEAD: Bettina Warscheid

PROVIDER: PXD004151 | Pride | 2017-01-02


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Myofibrillar Z-discs Are a Protein Phosphorylation Hot Spot with Protein Kinase C (PKCα) Modulating Protein Dynamics.

Reimann Lena L   Wiese Heike H   Leber Yvonne Y   Schwäble Anja N AN   Fricke Anna L AL   Rohland Anne A   Knapp Bettina B   Peikert Christian D CD   Drepper Friedel F   van der Ven Peter F M PF   Radziwill Gerald G   Fürst Dieter O DO   Warscheid Bettina B  

Molecular & cellular proteomics : MCP 20161227 3

The Z-disc is a protein-rich structure critically important for the development and integrity of myofibrils, which are the contractile organelles of cross-striated muscle cells. We here used mouse C2C12 myoblast, which were differentiated into myotubes, followed by electrical pulse stimulation (EPS) to generate contracting myotubes comprising mature Z-discs. Using a quantitative proteomics approach, we found significant changes in the relative abundance of 387 proteins in myoblasts <i>versus</i>  ...[more]

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