PXD009228

PXD009228 is an original dataset announced via ProteomeXchange.

Title	Phosphoproteomics Identifies Dual-Site Phosphorylation in an Extended Basophilic Motif Regulating FILIP1-mediated Degradation of filamin-C FLNc S2233 S2236 PRM analysis
Description	Skeletal muscle is known to adapt dynamically to changes in workload by regulatory processes of the phosphatidylinositide 3-kinase (PI3K)/Akt pathway. We performed a global quantitative phosphoproteomics analysis of contracting mouse C2 myotubes treated with insulin growth factor 1 (IGF-1) or LY294002 to activate or inhibit PI3K/Akt signaling, respectively. Among the significantly regulated phosphopeptides we identified the novel extended basophilic motif RxRxxp[S/T]xxp[S] to be enriched in the set of down-regulated phosphopeptides following inhibition of PI3K/Akt signaling. Using literature-based text mining we identified the kinases Akt, serum and glucocorticoid-regulated kinase 1 (SGK1) and p70S6 kinase to be potentially involved in the phosphorylation of the first serine in the RxRxxp[S/T]xxp[S] motif, whereas no kinase targeting the serine in the +3 position was revealed. In the signaling adapter protein filamin c (FLNc) we found this novel motif in immunoglobulin (Ig)-like domain 20 which is involved in various protein interactions. Through in vitro and in cellulo kinase assays we identified Akt and protein kinase C alpha as the responsible kinases phosphorylating FLNc in this motif at the first and the second serine, respectively.
HostingRepository	PRIDE
AnnounceDate	2020-06-30
AnnouncementXML	Submission_2020-06-30_02:15:28.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD009228
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Friedel Drepper
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: 10090;
ModificationList	Phospho; Oxidation
Instrument	Q Exactive

Revision	Datetime	Status	ChangeLog Entry
0	2018-03-16 04:06:10	ID requested
⏵ 1	2020-06-30 02:15:29	announced

Reimann L, Schw, ä, ble AN, Fricke AL, M, ü, hlh, ä, user WWD, Leber Y, Lohanadan K, Puchinger MG, Sch, ä, uble S, Faessler E, Wiese H, Reichenbach C, Knapp B, Peikert CD, Drepper F, Hahn U, Kreutz C, van der Ven PFM, Radziwill G, Djinovi, ć, -Carugo K, F, ü, rst DO, Warscheid B, Phosphoproteomics identifies dual-site phosphorylation in an extended basophilic motif regulating FILIP1-mediated degradation of filamin-C. Commun Biol, 3(1):253(2020) [pubmed]

curator keyword: Biological

submitter keyword: filamin C, Akt, PKC, myocytes

Bettina Warscheid
contact affiliation	Department of Biochemistry and Functional Proteomics, Institute of Biology II, Faculty of Biology and BIOSS Centre for Biological Signalling Studies, University of Freiburg, 79104 Freiburg im Breisgau, Germany
contact email	bettina.warscheid@biologie.uni-freiburg.de
lab head
Friedel Drepper
contact affiliation	AG Warscheid Biologie II Albert-Ludwigs-Universität Freiburg Schänzlestr. 1 79104 Freiburg Germany
contact email	friedel.drepper@biologie.uni-freiburg.de
dataset submitter

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PRIDE project URI

• PRIDE
  1. PXD009228
     1. Label: PRIDE project
     2. Name: Phosphoproteomics Identifies Dual-Site Phosphorylation in an Extended Basophilic Motif Regulating FILIP1-mediated Degradation of filamin-C FLNc S2233 S2236 PRM analysis