{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/WT-explants_report.tsv"],"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/WT-tissue-matrix.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/metadata-all.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/TurboID-explants-matrix.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/WT-explants-matrix.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/TurboID-compartments-matrix.csv"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/TurboID-compartments-search.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/TurboID-explants.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/fasta.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/WT-explants.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/WT-tissues.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/TurboID-compartments-quant.zip","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/04/PXD062198/TurboID-compartments.zip"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["manuela_schmidt@univie.ac.at"],"submitter":["Allison Barry"],"technology_type":["Mass Spectrometry","diaPASEF","Data-independent acquisition"],"software":[""],"submitter_keywords":["Dorsal root ganglia","Pns","Sensory neuron","Dia-ms","Turboid"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD062198"],"tissue":["Nerve","Spinal Ganglion","Spinal Cord","Skin"],"sample_protocol":["Adult TurboID x Adv-/Adv+ mice and wild type C57BL/6J male mice were kept in a 12/12h day/night cycle with ad libitum access to food and water in an open-cage environment. TurboID mice received biotin-enriched drinking water (0.22 mg/mL, prepared freshly every day) for 7 consecutive days and on day 8 the mice were sacrificed. All mouse work strictly followed the regulations. Mice were sacrificed via CO2-inhalation and rapidly decapitated. The vertebral spine was removed for subsequent isolation of the dorsal part of the lumbar 3-5 spinal cord (dLSC) and lumbar 3-5 dorsal root ganglia (DRG). In parallel the sciatic nerves (SCN) of both sides were dissected. The plantar paw skin (dermis and epidermis, without muscle tissue) was removed by a 4 mm skin punch. Skin samples were immediately snap-frozen in liquid N2, all other tissues were washed in ice-cold 1× PBS to remove blood residuals before snap-freezing in liquid N2. All tissues remained at -80°C until further use.  Tissue homogenisation was done in lysis buffer (LB; 2% SDS, 0.1 M tris, 5% glycerol, 0.01M DTT, 1× complete protease inhibitor cocktail). Extended details about tissue-specific lysis modifications (eg. acetone precipitation for the paw, SCN, and dLSC) and sample preparation can be found in the corresponding manuscript.  Streptavidin-mediated enrichment of biotinylated proteins : Streptavidin-affinity purification protocol is based on the high stringency protocol described in Go et al., 2021 with modifications. See methods for full details. Peptides were reconstituted in 20-25 µL MS-grade water, incubated for 5 min with shaking at 500 rpm, followed by another 2-min incubation on a magnetic rack. Peptide concentrations were measured at 205 nm with a NanoPhotometer, and samples were acidified to a final concentration of 0.1% formic acid (FA). The samples were stored at -20°C until LC-MS measurement.    DRG explants preparation: From both TurboID Adv+ and Adv- mice (fed with biotin-enriched water for 7 days, see above) 20 DRG per side were isolated and collected separately by side in two tubes containing DMEM/F-12 at RT. The DRG of one side were plated in 50 µL volume into a well of a 24-well plate and incubated for 10 min at 37°C, 5% CO2. In the meantime, the oxaliplatin (100nM) and/or vehicle (H2O, Veh) was mixed with DMEM +10% horse serum (HS) +100 ng/mL nerve growth factor (NGF) + 50 µM biotin and 500 µL/well were carefully added. The drug/veh was incubated for 48 h at 37°C, 5% CO2.   Sample preparation of DRG explants: The protein extraction was done similarly for both WT and TurboID DRG explants. All DRG of one well were transferred to an Eppendorf tube and washed twice with ice-cold 1× PBS by inverting the tube 10×. After discarding all PBS, 300 µL LB was added and DRG explants were sonicated for 10 cycles and further incubated at 70°C, for 15 min and 1500 rpm. Remaining cell debris was pelleted by centrifugation (5’, 10000×g) and the supernatant was saved. The total protein concentration was determined at 280nm with a NanoPhotometer N60. The TurboID samples underwent the above described streptavidin-affinity purification to enrich for biotinylated proteins and preparation of peptides (input 725 µg). For the WT samples a modified version of the SP3 method (Hughes et al., 2019) and similar to Xian et al., 2022 was employed to digest proteins and clean the peptides.   Nanoflow reversed-phase liquid chromatography (Nano-RPLC) was performed on NanoElute2 systems (Bruker Daltonik). This was coupled with timsTOF HT (Bruker Daltonik) via CaptiveSpray ion source. Mobile phase A consisted of 100% water, 0.1% formic acid (FA) and mobile phase B of 100% acetonitrile (ACN), 0.1% FA. Peptides were loaded onto a C18 trap column (1 mm x 5 mm, ThermoFisher) and further separated over a 90 min gradient on an AuroraTM ULTIMATE column (25 cm × 75 µm) packed with 1.6 µm C18 particles (IonOpticks). The flow rate was set to 250 nL/min, except for the last 7 minutes, where the flow rate was accelerated to 400 nL/min. The mobile phase B was linearly increased from 2 to 20% in the first 60 minutes, followed by another linear increase to 35% within 22 minutes and a steep increase to 85% in 0.5 min. Then, a flow rate switch to 400 nL/min was achieved in 0.5 min and was maintained for 7 minutes to the end of the gradient to elute all hydrophobic peptides.  The samples were analyzed in data-independent acquisition (DIA) mode coupled with parallel accumulation serial fragmentation (PASEF). Precursors with m/z between 350 and 1100 were defined in 13 cycles (either 2 or 3 quadrupole switches per cycle) containing 34 ion mobility steps within the ion mobility range of 0.65 – 1.35 (1/k0) with fixed isolation window of 25 Th in each step. The acquisition time of each DIA-PASEF scan was set to 100 ms, which led to a total cycle time of around 1.48 sec. The collision energy was ramped linearly from 65 eV at 1/k0 = 1.6 to 20 eV at 1/k0 = 0.6."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["DIA-NN 1.8.2 (Demichev et al., 2020) was used to process DIA-PASEF data in library-free mode. For the TurboID and WT samples, each tissue and, in case of TurboID Adv+/- also each genotype was processed in a separate analysis step using the same spectral library. The spectral library was predicted from a Mus musculus proteome database from UniProt containing 17,070 protein entries (downloaded on 2021-07-08), in case of the TurboID samples it included in addition streptavidin (P22629|SAV_STRAV) and TurboID sequence (Branon 2018). In silico digestion was performed using Trypsin/P, allowing up to two missed cleavages. A maximum of three variable modifications was allowed per peptide including methionine oxidation, and N-terminal acetylation, while Cysteine carbamidomethylation was set as a fixed modification. Peptide length for the search ranged from 5 to 52 amino acids. Precursor charge was set to 2-4. In accordance with the DIA-PASEF acquisition method, the m/z ranges were set to 350–1100 for precursor ions and 100–1700 for fragment ions. Mass accuracy was chosen automatically using the first run in the experiment. Protein inference was performed using unique genes. For neural network classifier the single-pass mode was chosen. Quantification was carried out using RT-dependent cross-run normalization and the Quant UMS (high precision) option. The main DIA-NN output was processed using the R package DiaNN (Demichev et al., 2020; Demichev, 2020) to extract MaxLFQ intensities (Cox et al., 2014) for all identified protein groups, applying a q-value threshold of <0.01 at both the precursor and gene group levels. Matrices were merged by protein group were applicable for downstream analyses."],"omics_type":["Proteomics"],"labhead":["Manuela Schmidt"],"instrument_platform":[""],"labhead_affiliation":["University of Vienna"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["10.1002/EJP.70277"],"submitter_mail":["allison.barry@univie.ac.at"],"submitter_affiliation":["University of Vienna"],"submitter_country":["Austria"],"additional_accession":[]},"is_claimable":false,"name":"A sub-compartment proteome for murine sensory neurons","description":"We applied TurboID-based proximity labelling restricted to Advillin-expressing neurons to systematically profile the proteomes of distinct neuronal subcompartments, using parallel accumulation–serial fragmentation combined with data-independent acquisition (diaPASEF) mass spectrometry. Neuronal compartments include somata (L3–L5 dorsal root ganglia, DRG), presynaptic terminals (dorsal lumbar spinal cord; dLSC), axons (sciatic nerve; SCN), and peripheral terminals (paw skin), providing the first proteomic atlas derived of/enriched in  lumbar sensory neurons. Our findings provide novel insights into the compartment-specific protein distributions that underlie key aspects of sensory neuron function.   To highlight to effectiveness of this approach. we also explored the neuronal proteome on DRG explants exposed to Oxaliplatin (or Vehicle) to extract neuron-specific changes upon chemotherapy exposure.  In both cases, the corresponding, wildtype (whole tissue) proteomes were also profiled with diaPASEF. Together, these data serve as a valuable resource for future studies on neuronal specialization and pain-related proteomic alterations in the 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