{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/eGFP_R2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/eGFP-RNAseT2_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/eGFP-RNAseT2_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/eGFP_R1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/eGFP_R3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/eGFP-RNAseT2_R2.raw"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/Result.mzid.gz"],"Mgf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/eGFP-RNAseT2_R1.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/eGFP_R2.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/eGFP-RNAseT2_R3.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/eGFP_R3.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/eGFP-RNAseT2_R2.mgf","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD045581/eGFP_R1.mgf"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["yohann.coute@cea.fr"],"submitter":["Yohann Couté"],"technology_type":["Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry"],"software":[""],"submitter_keywords":["Co-immunoprecipitation","Ribonuclease t2","Nanolc-ms/ms","Skeletal mucle injury","Muscle stem cells"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD045581"],"tissue":["Myoblast"],"sample_protocol":["C2C12 cells were grown in DMEM supplemented with 20% FBS and 1% PS. To generate a C2C12 cell line expressing an RNASET2-GFP fusion protein, C2C12 cells were transfected by pEGFP-N1-hRNAseT2 or control empty pEGFP-N1 (Clontech) plasmids with jetPRIME Transfection reagent (Polyplus) according to manufacturer’s instructions. Transfected cells were selected for one week with 0.5 mg/mL G418 and GFP+ cells were FACS-sorted on a BD FACSAria II and maintained in culture with 0.5 mg/mL G418. Three biological replicates were prepared for co-immunoprecipitation experiments from eGFP-RNAseT2 and eGFP expressing cells. Cells were seeded at 2,500 cells/cm2 in 10 cm dishes and grown in DMEM / 20% FBS / 1% PS / 0.5 m g/mL G418 for 4 days. Dishes were transferred on ice and washed twice in cold PBS containing 0.2 mM PMSF. Cells were lysed by scrapping in cold Lysis buffer (10 mM Tris pH 7.5 / 150 mM NaCl / 0.5 mM EDTA / 0.5% IGEPAL-CA630 / 1 mM PMSF / 1 mM B-glycerophosphate / 1 mM Na pyrophosphate / 1 mM Na Orthovanadate / 1% Protease inhibitor (Sigma #P8340)) and transferred into a cold 1.5 mL tube. After a 30 min incubation on ice, samples were centrifuged for 10 min at 13200 rpm at 4°C. Supernatant was transferred into a new cold 1.5 mL tube and diluted with 1.5 mL Dilution Buffer (10 mM Tris pH 7.5 / 150 mM NaCl / 0.5 mM EDTA / 1 mM PMSF / 1 mM B-glycerophosphate / 1 mM Na pyrophosphate / 1 mM Na Orthovanadate / 1% Protease inhibitor (Sigma #P8340)). Proteins were quantified using Pierce BCA Protein Assay Kit (Thermofisher). For immunoprecipitation, 4 mg of protein extracts were first pre-cleared with 80 L of Chromotek Binding Control Agarose Beads (Proteintech) for 30 min at 4°C on a rotating wheel. In order to pull down GFP or RNASET2-GFP fusion proteins, pre-cleared extracts were incubated with 80 L of Chromotek GFP-Trap Agarose Beads (Proteintech) for 1 h at 4°C on a rotating wheel. Beads were washed 3 times in Dilution Buffer for 10 min at 4°C on a rotating wheel and proteins were eluted in 2X Laemmli buffer. Proteins solubilized in Laemmli buffer were stacked in the top of a 4-12% NuPAGE gel (Invitrogen), stained with Coomassie blue R-250 (Bio-Rad) before in-gel digestion using modified trypsin (Promega, sequencing grade). The resulting peptides were analyzed by online nanoliquid chromatography coupled to MS/MS (Ultimate 3000 RSLCnano and Q-Exactive HF, Thermo Fisher Scientific) using 120 min acetonitrile gradient. For this purpose, the peptides were sampled on a precolumn (300 μm x 5 mm PepMap C18, Thermo Scientific) and separated in a 75 μm x 250 mm C18 column (Reprosil-Pur 120 C18-AQ, 1.9 μm, Dr. Maisch). The MS and MS/MS data were acquired using Xcalibur 2.8 (Thermo Fisher Scientific)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Peptides and proteins were identified by Mascot (version 2.7.0.1, Matrix Science) through concomitant searches against the Uniprot database (Mus musculus taxonomy, September 2020 version), a homemade database containing the sequences of classical contaminant proteins found in proteomic analyses (human keratins, trypsin...), and the corresponding reversed databases. Trypsin/P was chosen as the enzyme and two missed cleavages were allowed. Precursor and fragment mass error tolerances were set at respectively at 10 and 20 ppm. Peptide modifications allowed during the search were: Carbamidomethyl (C, fixed), Acetyl (Protein N-term, variable) and Oxidation (M, variable). The Proline software (version 2.1.0) was used for the compilation, grouping, and filtering of the results: conservation of rank 1 peptides, peptide score ≥ 25, peptide length ≥ 7 amino acids, peptide-spectrum-match identification false discovery rate < 1% as calculated on scores by employing the reverse database strategy, and minimum of 1 specific peptide per identified protein group."],"omics_type":["Proteomics"],"labhead":["Yohann Couté"],"instrument_platform":[""],"labhead_affiliation":["EDyP"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"submitter_mail":["yohann.coute@cea.fr"],"publication":["41980967 Weiss-Gayet M, Juban G, Le Moal E, Moretta A, Farnetani C, Gobet C, Guillemaud J, Le Bihan MC, Shoseyov O, Adrait A, Ternka K, Boespflug-Tanguy O, Kettwig M, Couté Y, Mounier R, Acquati F, Knight RD, Chazaud B. Restorative macrophage-derived RNAseT2 stimulates muscle stem cell fusion via an SLK/N-WASP/actin bundling dependent axis. Nat Commun. 2026 17(1):5199 10.1038/s41467-026-71990-z"],"submitter_affiliation":["EDyP"],"submitter_country":["France"],"doi":["10.6019/PXD045581"],"pubmed_abstract":["Muscle stem cells (MuSCs) fuse to form myofibers to repair skeletal muscle after injury. Within the regenerative MuSC niche, restorative macrophages stimulate MuSC fusion, although the molecular mechanisms involved are largely unknown. Here, we show that restorative macrophages secrete ribonuclease T2 (RNAseT2) to stimulate MuSC fusion. RNAseT2 enters MuSCs via the mannose receptor and induces the formation of actin bundles in MuSCs, enabling cell/cell fusion. Mechanistically, RNAseT2 binds to Ste20-like kinase (SLK), which itself triggers the phosphorylation-mediated activation of N-WASP, through Paxillin phosphorylation, allowing actin bundling necessary for MuSC fusion. In vivo, overexpressing RNAseT2 in regenerating muscle increases fusion in newly formed myofibers in mouse and zebrafish while macrophages deficient for RNAseT2 gene lead to fusion defect and smaller myofibers. This study reveals a new function for the highly conserved RNAseT2 and provides a new molecular mechanism by which restorative macrophages support MuSC fusion during muscle repair."],"pubmed_title":["Restorative macrophage-derived RNAseT2 stimulates muscle stem cell fusion via an SLK/N-WASP/actin bundling dependent axis."],"pubmed_authors":["Weiss-Gayet Michéle M, Juban Gaëtan G, Le Moal Emmeran E, Moretta Antonio A, Farnetani Camilla C, Gobet Christelle C, Guillemaud Jules J, Le Bihan Marie-Catherine MC, Shoseyov Oded O, Adrait Annie A, Ternka Katharina K, Boespflug-Tanguy Odile O, Kettwig Matthias M, Couté Yohann Y, Mounier Rémi R, Acquati Francesco F, Knight Robert D RD, Chazaud Bénédicte B"],"additional_accession":[]},"is_claimable":false,"name":"Characterization of RNAseT2 interactome in C2C12 cells","description":"Muscle stem cells (MuSCs) fuse to form multinucleated cells to repair skeletal muscle after injury. While adult MuSCs express a cell autonomous myogenesis program, in vivo investigations demonstrated that the MuSC environment is required for efficient adult myogenesis and muscle regeneration. Particularly, anti-inflammatory/restorative macrophages stimulate MuSC differentiation and fusion, although the molecular mechanisms involved are still largely unknown. Here, we show that restorative macrophages secrete ribonuclease T2 (RNAseT2) which specifically stimulates MuSC fusion. Co-immuprecipitation coupled to mass spectrometry-based proteomics identified Ste20-like kinase (SLK) as binding partner of RNAseT2. SLK triggered the phosphorylation-mediated activation of N-WASP, allowing actin remodeling at the time of MuSC 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