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Proteomics

Dataset Information

55

In vitro calpainolysis assays - Myofibrillar Z-discs are a protein phosphorylation hot spot with PKC α modulating protein dynamics


ABSTRACT: In vitro calpainolysis in combination with top down mass spectrometry reveals the calpain-1 cleavage sites in human and murine carboxy terminal regions of FLNc

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Homo sapiens   Mus musculus  

TISSUE(S): Tissue Not Applicable To Dataset

DISEASE(S): Not Available

SUBMITTER: Friedel Drepper  

LAB HEAD: Bettina Warscheid

PROVIDER: PXD003216 | Pride | 2017-01-02

REPOSITORIES: pride

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Publications

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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