Proteomics

Dataset Information

0

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

REPOSITORIES: Pride

Json Xml
altmetric image

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]

Similar Datasets

Transcriptomics Transcriptomic and proteomic profiling of KEAP1 disrupted and sulforaphane treated human breast epithelial cells
2011-04-22 | E-GEOD-28813 | biostudies-arrayexpress
Transcriptomics Saccharomyces cerevisiae mutant strain with R1158 strain background: Fold change after doxycycline treatment
2014-03-26 | E-GEOD-56186 | biostudies-arrayexpress
Proteomics SILAC quantification of proteins in the control and UFBP1-expressing MGC803 cells
2021-02-15 | PXD013590 | Pride
Proteomics Quantitative phosphoproteome of contracting C2 myotubes with pharmacological intervention of the PI3K-AKT-mTOR-S6K and RAF-MEK-ERK-RSK cascades
2023-02-22 | PXD018667 | Pride
Proteomics Metformin impairs cisplatin effects in cell size and proliferation of A549 lung cancer cells, modulating the mTOR and other metabolic pathways.
2021-09-09 | PXD017645 | Pride
Proteomics PKA-Independent Vasopressin Signaling in Renal Collecting Duct
2020-03-05 | PXD015719 | Pride
Proteomics Identification of RNA binding proteins that interact with AU-rich elements of Lif 3`UTR
2016-07-20 | PXD001463 | Pride
Proteomics CRISPR/Cas9-mediated knockout and endogenous complex analysis of Cluap1/ IFT38
2018-04-04 | PXD008343 | Pride
Proteomics Phosphatase POPX2 secretome SILAC
2019-10-21 | PXD001618 | Pride
Proteomics Identification of immunoglobulin switch (S) region binding proteins by insertional ChIP (iChIP)
2020-06-15 | PXD019042 | Pride