PXD053234 is an
original dataset announced via ProteomeXchange.
Dataset Summary
Title | Human FLNc-S2233/S2236 phosphorylation after EPS treatment (PRM analysis) |
Description | The actin-binding protein filamin c (FLNc) is a key mediator in the response of skeletal muscle cells to mechanical stress. In addition to its function as a structural scaffold, FLNc acts as a signaling adaptor which is phosphorylated at S2234 in its mechanosensitive domain 20 (d20) through AKT. Here, we discovered a strong dephosphorylation of FLNc-pS2234 in skeletal myotubes under acute mechanical stress, despite high AKT activity. We found that all three protein phosphatase 1 (PP1) isoforms are part of the FLNc d18-21 interactome. Enzymatic assays demonstrate that PP1 efficiently dephosphorylates FLNc-pS2234 in vitro and in cells upon PP1 activation using specific modulators. FLNc-pS2234 dephosphorylation promotes the interaction with FILIP1, a mediator for filamin degradation. Collectively, we present a model in which dephosphorylation of FLNc d20 by the dominant action of PP1c prevails over AKT activity to promote the binding of the filamin degradation-inducing factor FILIP1 during acute mechanical stress. Note that mouse FLNc S2234/S2237 correspond to S2233 and S2236 in human FLNc. |
HostingRepository | PRIDE |
AnnounceDate | 2025-05-07 |
AnnouncementXML | Submission_2025-05-06_19:33:58.591.xml |
DigitalObjectIdentifier | |
ReviewLevel | Peer-reviewed dataset |
DatasetOrigin | Original dataset |
RepositorySupport | Unsupported dataset by repository |
PrimarySubmitter | Julian Bender |
SpeciesList | scientific name: Mus musculus (Mouse); NCBI TaxID: 10090; |
ModificationList | phosphorylated residue; acetylated residue; iodoacetamide derivatized residue |
Instrument | Q Exactive Plus |
Dataset History
Revision | Datetime | Status | ChangeLog Entry |
0 | 2024-06-19 03:34:52 | ID requested | |
⏵ 1 | 2025-05-06 19:33:59 | announced | |
Publication List
Kokot T, Zimmermann JP, Schw, ä, ble AN, Reimann L, Herr AL, H, ö, fflin N, K, ö, hn M, Warscheid B, Protein phosphatase-1 regulates the binding of filamin C to FILIP1 in cultured skeletal muscle cells under mechanical stress. Sci Rep, 14(1):27348(2024) [pubmed] |
10.1038/s41598-024-78953-8; |
Keyword List
submitter keyword: Phosphoproteomics, C2 cells,Targeted MS, PRM, Skyline, Mechanical stress |
Contact List
Bettina Warscheid |
contact affiliation | Chair of Biochemistry II, Theodor Boveri-Institute, Biocenter, University of Würzburg, Würzburg, Germany |
contact email | bettina.warscheid@uni-wuerzburg.de |
lab head | |
Julian Bender |
contact affiliation | University of Wuerzburg
Chair of Biochemistry II
Am Hubland
97074 Würzburg |
contact email | julian.bender@uni-wuerzburg.de |
dataset submitter | |
Full Dataset Link List
Dataset FTP location
NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2025/05/PXD053234 |
PRIDE project URI |
Repository Record List
[ + ]
[ - ]
- PRIDE
- PXD053234
- Label: PRIDE project
- Name: Human FLNc-S2233/S2236 phosphorylation after EPS treatment (PRM analysis)