Dataset Information

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

ACCESS DATA

Dataset's files

Source:

Items per page:

1 - 5 of 14

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

			Action	DRS
	ELITE-RSLC000958.raw	Raw
	ELITE-RSLC000960.raw	Raw
	ELITE-RSLC013486.raw	Raw
	ELITE-RSLC013487.raw	Raw
	ELITE-RSLC013490.raw	Raw

Dataset Information

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

Dataset's files

Publications

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

Similar Datasets

OmicsDI is part of the ELIXIR infrastructure

Tweets

Similar Datasets

FilaminC pull-down experiment from myotube lysates
2020-05-25 | PXD017670 | Pride

C-terminal FLNc in vivo kinase assay
2017-01-02 | PXD004151 | Pride

Homozygous expression of the myofibrillar myopathy-associated p.W2710X filamin C variant reveals major pathomechanisms of sarcomeric lesion formation
2020-09-09 | PXD020097 | Pride

FLNc Calpain GluC SRM Analysis
2017-01-02 | PXD005097 | Pride

In vitro calpainolysis assays - Myofibrillar Z-discs are a protein phosphorylation hot spot with PKC α modulating protein dynamics
2017-01-02 | PXD003216 | Pride

Filamin C domain 18-21 in vitro kinase assay
2020-05-25 | PXD008893 | Pride

Large-scale in vitro kinase assay with FLNc d23-24 and PKC alpha
2017-01-02 | PXD003185 | Pride

First Clinical and Myopathological Description of a Myofibrillar Myopathy with Congenital Onset and Homozygous Mutation in FLNC
2020-07-24 | PXD016657 | Pride

Molecular basis of F-actin regulation and sarcomere assembly via myotilin
2021-02-22 | PXD024301 | Pride