{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/proteinGroups.txt","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/120mins_OTIT_FusionMS_TM_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/120mins_OTIT_FusionMS_Ctrl_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/120mins_OTIT_FusionMS_Inhib_TM_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/120mins_OTIT_FusionMS_Ctrl_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/120mins_OTIT_FusionMS_TM_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/120mins_OTIT_FusionMS_Inhib_TM_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/120mins_OTIT_FusionMS_TM_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/120mins_OTIT_FusionMS_Inhib_TM_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/120mins_OTIT_FusionMS_TM_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/120mins_OTIT_FusionMS_Ctrl_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/120mins_OTIT_FusionMS_Inhib_TM_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD059735/120mins_OTIT_FusionMS_Ctrl_4.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["brian.mcdonagh@universityofgalway.ie"],"submitter":["Brian McDonagh"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Perk amg44","Er stress","Tunicamycin","Skeletal muscle"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD059735"],"tissue":["Skeletal Muscle Myoblast","Cell Culture"],"sample_protocol":["Proteomics was performed on protein extracts from C2C12 myoblasts homogenised in 50 mM ammonium acetate containing 1% RapiGest. Protein lysates were centrifuged at 15,000 g for 10 min at 4 °C and protein concentrations were determined using Bradford assay with BSA as the standard. Trypsin was reconstituted in 50 mM acetic acid, and 2 μg was added to the 100 μg of protein from samples, followed by overnight incubation at 37 °C. The digestion was stopped and RapiGest removed by acidification (3 μL of TFA and incubation at 37 °C for 45 min) and centrifugation (15,000 g for 15 min.  Mass spectrometry analysis was performed at the proteomics facility NICB at Dublin City University. For LC-MS/MS analysis, an UltiMate 3000 RSLCnano LC system was coupled to an Orbitrap FusionTM mass spectrometer (Thermo Fisher Scientific). Peptides were loaded onto a trap column (AcclaimTM Pep-MapTM 100C18 LC Columns 5 μm, 20 mm length) for 3 min at a flow rate of 10 μL/min in 0.1% formic acid (FA). Subsequently, peptides were transferred to an EASY-Spray PepMap RSLC C18 column (Thermo) (2 μm, 75 μm × 50 cm) operated at 45 °C and separated using a 60-minute gradient (buffer A: 0.1% FA; buffer B: 100% ACN, 0.1% FA) at a flow rate of 250 nL/min. The gradient ranged from 2% to 6% of buffer B in 2 min, from 6% to 33% B in 58 min, from 33% to 45% in 2 min, and held at 98% B for an additional 10 min. Peptides were ionised at 1.5 kV into the mass spectrometer via the EASY-Spray source, with a capillary temperature set to 300 °C. The mass spectrometer operated in a data-dependent mode, with automatic switching between MS and MS/MS scans using a top 18 method (intensity threshold ≥3.6e5, dynamic exclusion of 20 seconds, and excluding charges  +1 and > +6). MS spectra were acquired from 350 to 1400 m/z with a resolution of 60,000 FWHM (200 m/z). Peptide ions were isolated with a 1.0 Th window and fragmented using higher-energy collisional dissociation (HCD) with a normalised collision energy of 29. MS/MS spectra resolution was set to 15,000 (200 m/z). The normalised AGC ion target values were 300% for MS (maximum ion time of 25 ms) and 100% for MS/MS (maximum ion time of 22 ms)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Mass spectrometry data was analysed for global changes in protein abundance. Raw files were processed using MaxQuant (v 1.6.0.16) against a Mus musculus protein database (UniProtKB/Swiss-Prot/TrEMBL, n sequences). Variable modifications included N-ethylmaleimide and D5 N-ethylmaleimide on Cysteine, oxidation of Methionine, and protein N-terminal acetylation. Minimal peptide length was set to 7 amino acids, and a maximum of two tryptic missed cleavages were allowed. Results were filtered at 0.01 false discovery rate (FDR) at both peptide and protein levels. The \"proteinGroups.txt\" file was analysed using Prostar software [65]. Proteins with fewer than three valid values in at least one experimental condition were filtered out. A global normalisation of log2-transformed intensities across samples was performed using the local weighted regression (LOESS). Missing values were imputed using the structured least squares algorithm (SLSA) for partially observed values and DetQuantile for values missing from an entire condition. Differential analysis was conducted using the empirical Bayes statistics Limma. Proteins with a p value < 0.01 and a Log2FC ratio > 0.58 or < -0.58 (FC > 1.5) were considered significantly changed, with an estimated FDR below 6.5% by Benjamini-Hochberg."],"omics_type":["Proteomics"],"labhead":["Brian McDonagh"],"instrument_platform":[""],"labhead_affiliation":["Physiology, University of Galway, Ireland"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["41176528 Casas-Martinez JC, Xia Q, Li P, Borja-Gonzalez M, Miranda-Vizuete A, McDermott E, Dockery P, Quinlan LR, Goljanek-Whysall K, Samali A, McDonagh B. Adaptive ER stress promotes mitochondrial remodelling and longevity through PERK-dependent MERCS assembly. Cell Death Differ. 2026 33(4):732-747 10.1038/s41418-025-01603-7"],"submitter_mail":["brian.mcdonagh@universityofgalway.ie"],"submitter_affiliation":["University of Galway"],"submitter_country":["Ireland"],"pubmed_abstract":["The transfer of information and metabolites between the mitochondria and the endoplasmic reticulum (ER) is mediated by mitochondria-ER contact sites (MERCS), allowing adaptations in response to changes in cellular homeostasis. MERCS are dynamic structures essential for maintaining cell homeostasis through the modulation of calcium transfer, redox signalling, lipid transfer, autophagy and mitochondrial dynamics. Under stress conditions such as ER protein misfolding, the Unfolded Protein Response (UPR<sup>ER</sup>) mediates PERK and IRE1 activation, both of which localise at MERCS. Adaptive UPR<sup>ER</sup> signalling enhances mitochondrial function and calcium import, whereas maladaptive responses lead to excessive calcium influx and apoptosis. In this study, induction of mild acute ER stress with tunicamycin (TM) in myoblasts promoted myogenesis that required PERK for increased MERCS assembly, mitochondrial turnover and function. Similarly, treatment of C. elegans embryos with an acute low concentration of TM, promoted an extension in lifespan and health-span. The adaptive ER stress response following a low dose of TM in both myoblasts and C. elegans, increased MERCS assembly and activated autophagy machinery, ultimately promoting an increase in mitochondrial remodelling. However, these beneficial adaptations were dependent on the developmental stage, as treatment of myotubes or adult C. elegans resulted in a maladaptive response. In both models the adaptations to UPR<sup>ER</sup> activation were dependent on PERK signalling and its interaction with the UPR<sup>mt</sup>. The results demonstrate PERK is required for the increased mitochondrial ER communication in response to adaptive UPR signalling, promoting mitochondrial remodelling and improved physiological function."],"pubmed_title":["Adaptive ER stress promotes mitochondrial remodelling and longevity through PERK-dependent MERCS assembly."],"pubmed_authors":["Casas-Martinez Jose C JC, Xia Qin Q, Li Penglin P, Borja-Gonzalez Maria M, Miranda-Vizuete Antonio A, McDermott Emma E, Dockery Peter P, Quinlan Leo R LR, Goljanek-Whysall Katarzyna K, Samali Afshin A, McDonagh Brian B"],"additional_accession":[]},"is_claimable":false,"name":"Proteomic analysis of C2C12 myoblasts treated with Tunicamycin","description":"Label free proteomic analysis of C2C12 myoblasts treated with either Tunicamycin (0.2ug/ml) alone or with PERK AMG44 (2uM) for 8h and followed by 16h 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