PXD053234-1

PXD053234 is an original dataset announced via ProteomeXchange.

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

Revision	Datetime	Status	ChangeLog Entry
0	2024-06-19 03:34:52	ID requested
⏵ 1	2025-05-06 19:33:59	announced

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;

submitter keyword: Phosphoproteomics, C2 cells,Targeted MS, PRM, Skyline, Mechanical stress

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

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

• PRIDE
  1. PXD053234
     1. Label: PRIDE project
     2. Name: Human FLNc-S2233/S2236 phosphorylation after EPS treatment (PRM analysis)