Dataset Information

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

TISSUE(S): Skeletal Muscle Cell, Skeletal Muscle Cell Line

SUBMITTER: Friedel Drepper

LAB HEAD: Bettina Warscheid

PROVIDER: PXD008875 | Pride | 2022-06-06

REPOSITORIES: Pride

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Publications

Phosphoproteomics identifies dual-site phosphorylation in an extended basophilic motif regulating FILIP1-mediated degradation of filamin-C.

Reimann Lena L Schwäble Anja N AN Fricke Anna L AL Mühlhäuser Wignand W D WWD Leber Yvonne Y Lohanadan Keerthika K Puchinger Martin G MG Schäuble Sascha S Faessler Erik E Wiese Heike H Reichenbach Christa C Knapp Bettina B Peikert Christian D CD Drepper Friedel F Hahn Udo U Kreutz Clemens C van der Ven Peter F M PFM Radziwill Gerald G Djinović-Carugo Kristina K Fürst Dieter O DO Warscheid Bettina B

Communications biology 20200522 1

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]

PMID: 32444788

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