Proteomics

Dataset Information

3

FILIP1 CT pull-down


ABSTRACT: FILIP1 was identified as potential new filamin C interaction partner by a SILAC-based BioID experiment. Interaction of the two protein via the carboxy-terminal end of FILIP and domain 18-21 of filamin C was prooven by yeast-2-hybrid sreens and dot-blot assays, respectively. To verify this interaction by mass spectrometry, recombinantly expressed FILIP1 carboxy-term was fused via its His6-tag to Ni2+-NTA beads. Subsequently. beads were incubated with cell extracts from human skeletal muscle cells. Bands observed in SDS-PAGE from the pull-down assay were cut and analysed by LC-MS. As a result Filamin C could be identified as FILIP1 binding partner.

INSTRUMENT(S): Q Exactive Plus

ORGANISM(S): Mus musculus  

TISSUE(S): Skeletal Muscle Cell Line

DISEASE(S): Not Available

SUBMITTER: Friedel Drepper  

LAB HEAD: Bettina Warscheid

PROVIDER: PXD008875 | Pride | 2022-06-06

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
QEplus018193.dat Other
QEplus018193.mzid.gz Mzid
QEplus018193.mzid_QEplus018193.MGF Mzid
QEplus018193.raw Raw
QEplus018195.dat Other
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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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