{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["14(1)"],"submitter":["Kokot T"],"pubmed_abstract":["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 cultured 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 and in vitro and in cells upon PP1 activation using specific modulators. FLNc-pS2234 dephosphorylation promotes the interaction with FILIP1, a mediator for filamin degradat"],"journal":["Scientific reports"],"pagination":["27348"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC11550807"],"repository":["biostudies-literature"],"pubmed_title":["Protein phosphatase-1 regulates the binding of filamin C to FILIP1 in cultured skeletal muscle cells under mechanical stress."],"pmcid":["PMC11550807"],"pubmed_authors":["Zimmermann JP","Kokot T","Hofflin N","Schwable AN","Herr AL","Warscheid B","Reimann L","Kohn M"],"additional_accession":[]},"is_claimable":false,"name":"Protein phosphatase-1 regulates the binding of filamin C to FILIP1 in cultured skeletal muscle cells under mechanical stress.","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 cultured 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 and in vitro and in cells upon PP1 activation using specific modulators. FLNc-pS2234 dephosphorylation promotes the interaction with FILIP1, a mediator for filamin degradat","dates":{"release":"2024-01-01T00:00:00Z","publication":"2024 Nov","modification":"2026-06-02T03:40:06.581Z","creation":"2025-04-04T12:01:22.902Z"},"accession":"S-EPMC11550807","cross_references":{"pubmed":["39521905"],"doi":["10.1038/s41598-024-78953-8"]}}