Proteomics

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Phosphoproteomics Identifies Dual-Site Phosphorylation in an Extended Basophilic Motif Regulating FILIP1-mediated Degradation of filamin-C FLNc d18-21 BioID experiment

ABSTRACT: FLNc, the muscle-specific isoform of the filamin family, is a multi-adaptor protein, comprising 1 amino-terminal actin-binding (ABD) domain followed by 24 immunoglobulin-like (Ig) domains. While FLNc can form homodimers via the last Ig-like domain and thus function as an actin-crosslinker like the other filamins, it features a unique insertion of 82 amino acids (aa) in domain 20. This insert was not only shown to mediate the interaction to several FLNc binding partners, but also to contain an Akt-mediated phosphorylation site at S2234 of mouse FLNc (mFLNc). To reveal novel proteins in the nano-environment of FLNc within myotubes under mild electrical pulse stimulation conditions, we applied a quantitative BioID appraoch.

INSTRUMENT(S): LTQ Orbitrap Elite

ORGANISM(S): Mus Musculus (mouse)

TISSUE(S): Skeletal Muscle Fiber, Myotube

SUBMITTER: Friedel Drepper  

LAB HEAD: Bettina Warscheid

PROVIDER: PXD009159 | Pride | 2021-07-12

REPOSITORIES: Pride

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Publications

The PI3K/Akt pathway promotes skeletal muscle growth and myogenic differentiation. Although its importance in skeletal muscle biology is well documented, many of its substrates remain to be identified. We here studied PI3K/Akt signaling in contracting skeletal muscle cells by quantitative phosphoproteomics. We identified the extended basophilic phosphosite motif RxRxxp[S/T]xxp[S/T] in various proteins including filamin-C (FLNc). Importantly, this extended motif, located in a unique insert in Ig-  ...[more]

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