{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/report.pg_matrix_LJ260326.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/2026-03-24_LJ_MFN2_Het-2-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/2026-03-24_LJ_MFN2_IgG-3-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/2026-03-24_LJ_MFN2_IgG-2-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/2026-03-24_LJ_MFN2_Het-1-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/2026-03-24_LJ_MFN2_Het-3-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/2026-03-24_LJ_MFN2_IgG-1-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/2026-03-24_LJ_MFN2_WT-1-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/2026-03-24_LJ_MFN2_WT-2-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/2026-03-24_LJ_MFN2_WT-3-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/2026-03-24_LJ_MFN2_KO-1-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/2026-03-24_LJ_MFN2_KO-3-01.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD077751/2026-03-24_LJ_MFN2_KO-2-01.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["mark.collins@sheffield.ac.uk"],"submitter":["Mark Collins"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Mitofusin-2","Mitochondria","Charcot-marie-tooth disease type 2a"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077751"],"tissue":["Cell Culture","Embryonic Stem Cell"],"sample_protocol":["Mass spectrometry analysis of MFN2 immunoprecipitations.  25 µl of IP elutions (5% SDS/50 mM Tris, pH 7.4), were reduced with TCEP to a final concentration of 5 mM and heated at 70 °C for 15 minutes. Proteins were alkylated by adding Iodoacetamide (IAA) to a final concentration of 10 mM, and the samples were incubated at 37 °C in the dark for 30 minutes. 2.5 µl of 12 % phosphoric acid and 165 µl of S-Trap binding buffer (90% methanol, 100 mM TEAB, pH 7.1) were then added to each sample. Samples were then loaded into S-Trap columns (ProtiFi) by centrifugation at 10,000 x g for 60 seconds. Samples were washed four times with 225 µl of S-Trap binding buffer through centrifugation at 10,000 x g for 60 seconds. 1 µg of Trypsin (Pierce, sequencing grade) was added to each sample in a total digestion volume of 20 µl of 50 mM TEAB, and digestion was performed at 47 °C for 1 hour, followed by 37 °C for 1 hour.  Peptides were eluted with the addition of 40 µl of 50 mM TEAB, 40 µl of 0.2% aqueous formic acid, and then 40 µl of 50% acetonitrile with 0.2% formic acid, followed by centrifugation at 10,000 x g for 60 seconds for each elution. Pooled eluted peptides were dried in a vacuum concentrator and resuspended in 0.5% formic acid for LC-MS/MS analysis. Each sample was analysed using nanoflow LC-MS/MS using an Orbitrap Exploris 480 (Thermo Fisher) mass spectrometer equipped with an EASY-Spray source coupled to a Vanquish LC System (Thermo Fisher). Peptides were desalted online using a Pepmap Neo C18 nano trap column, 300 μm I.D. x 5 mm (Thermo Fisher) and then separated using an EASY-Spray column, 50 cm × 75 μm ID, PepMap Neo C18, 2 μm particles, 10 Å pore size (Thermo Fisher) and separated using a 70-minute gradient. The Orbitrap Exploris 480 was operated in positive mode using a Velocity DIA method. MS1 spectra were acquired at a resolution of 60,000 at m/z 200 with a normalised AGC target of 300%. For the DIA analysis, multiply charged precursors in 40 m/z bins (400-900 mz range) were accumulated with a normalised AGC target of 800%, subjected to HCD fragmentation (145-1500 m/z) with a collision energy of 30%."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw mass spectrometry data files were processed with DIA-NN version 2.3.0. Data were analysed in library-free mode using a peptide library predicted from a Human proteome Fasta file (downloaded Aug 2025) containing 20475 proteins. The following settings were used in library prediction. Trypsin was set as the protease, with a maximum of 1 missed cleavage. Cysteine carbamidomethylation was enabled as a fixed modification. Maximum number of variable modifications set to 1 and acetyl-protein N term set as a variable modification. An FDR of 1% used for identification-level cut-offs. The DIA-NN output was loaded into Perseus version 1.6.10.50, and the matrix was filtered to remove all proteins that were potential contaminants and decoy hits. LFQ intensities were log2(x)- transformed, and data were filtered to retain proteins with at least 3 valid LFQ intensities in one group. Data were normalised by subtracting column medians, and missing values were imputed from the normal distribution with a width of 0.3 and downshift of 1.8. To identify quantitatively enriched proteins in MFN2 IPs versus control IPs, two-sided Student’s t-tests were performed with a permutation-based FDR of 0.05 with an S0 = 0.5. To identify differences in MFN2 interactions between mutant and wild type, LFQ intensities were instead normalised to the bait protein and two-sided Student’s t-tests were performed with a permutation-based FDR of 0.05 with an S0 = 0.5."],"omics_type":["Proteomics"],"labhead":["Mark Collins"],"instrument_platform":[""],"labhead_affiliation":["School of Biosciences Firth Court, Western Bank University of Sheffield"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["mark.collins@sheffield.ac.uk"],"submitter_affiliation":["University of Sheffield"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"HDAC6 inhibition alleviates mitochondrial trafficking in novel models of Charcot-Marie-Tooth Disease Type 2A","description":"Charcot-Marie-Tooth Disease (CMT) is a group of inherited progressive conditions affecting distal motor and sensory neurons, leading to muscle weakness, pain and loss of sensation in limbs. CMT type 2A (CMT2A) is the most common form of axonal CMT and is associated with a more severe clinical manifestation. However, there are no treatments currently available. To investigate disease mechanisms and facilitate treatment discovery, we developed an in vitro model for CMT2A by introducing the patient-specific MFN2R94Q/+ variant into human embryonic stem cells (hESCs). Isogenic variant and wild-type hESCs differentiated to spinal motor neurons with similar efficiency and gave rise to functional motor neurons in vitro. However, MFN2R94Q/+ spinal motor neurons displayed impaired mitochondrial trafficking, resulting in altered distribution of mitochondria in axons. To identify the molecular basis of these defects, we performed an unbiased quantitative proteomic screen of the endogenous MFN2 interactome, which revealed candidate MFN2 interactors implicated in MFN2-mediated regulatory signalling, cytoskeletal scaffolding, and ubiquitin-ligase machinery. Importantly, we showed that mitochondrial trafficking defects can be alleviated by treatment with an HDAC6 inhibitor. Chemical inhibition of HDAC6 also significantly rescued the motor phenotype in a zebrafish CMT2A model. Taken together, our study reveals a variant-specific insight into CMT2A disease mechanisms and confirms HDAC6 as a promising target for further therapeutic 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