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Label-free global phosphoproteomics experiment using PI3K-AKT-mTOR-S6K and RAF-MEK-ERK-RSK pathway activation and inhibition

ABSTRACT: The signaling network of skeletal muscle cells is controlled by a variety of protein kinases. Although many kinases are known players, their downstream targets are still largely unexplored. To gain further knowledge about the PI3K-AKT-mTOR-S6K and the RAF-MEK-ERK-RSK signaling networks in myotubes, we analyzed changes in protein phosphorylation levels upon pathway activation and direct kinase inhibition on a global scale. Based on the phosphoproteomics data, we further examined target relationships of the basophilic kinases AKT, RSK and S6K, which share the substrate recognition motif RxRxxp[ST].

INSTRUMENT(S): Q Exactive

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Cell Culture

SUBMITTER: Friedel Drepper

LAB HEAD: Prof. Dr. Bettina Warscheid

PROVIDER: PXD029678 | Pride | 2023-02-22

REPOSITORIES: Pride

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Quantitative phosphoproteome of contracting C2 myotubes with pharmacological intervention of the PI3K-AKT-mTOR-S6K and RAF-MEK-ERK-RSK cascades

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BI-D1870 is a specific inhibitor of the p90 RSK (ribosomal S6 kinase) isoforms in vitro and in vivo.

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