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Kalocsay"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"disease":["Sensory Peripheral Neuropathy"],"software":["Not available"],"submitter_keywords":["Ste20 kinases","High-throughput screening","Axon degeneration","Neuroprotective small molecules","Chemotherapy-induced peripheral neuropathy","Ipsc-derived sensory neurons"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074954"],"tissue":["Brain","Sensory Processing Neuron"],"sample_protocol":["Protein extraction and preparation Cells were lysed directly in sodium dodecyl sulfate (SDS)-based lysis buffer composed of 2% (w/v) SDS, 150 mM sodium chloride (NaCl), and 50 mM Tris (pH 8.7), supplemented with protease and phosphatase inhibitors (Thermo Fisher, Cat. #A32953 and #A32957). Following lysis, homogenization was carried out using Qiashredder spin columns (Qiagen, Cat. No. 79656) to ensure uniformity. Disulfide bonds were reduced by adding dithiothreitol (DTT) to a final concentration of 5 mM, followed by incubation at 37°C for 1 hour. Subsequently, cysteine residues were alkylated using 20 mM iodoacetamide in the dark, and the reaction was quenched by adding DTT to a final concentration of 50 mM. Protein concentration was quantified using the BCA Protein Assay Kit (Thermo Fisher Scientific, Cat. No. 23235) according to the manufacturer’s instructions. For each biological replicate, 2 mg of total protein was taken forward for subsequent processing. Detergents were removed from lysates using methanol/chloroform precipitation following the protocol described by Wessel, D.M. and Flügge, U.I., 1984 The resulting protein pellets were resolubilized in 8 M urea prepared in 200 mM EPPS buffer (pH 8.5). Proteins were digested in a two-step protocol. For each sample, Lys-C protease (2 mg/ml, Fujifilm Wako, Cat. #129-02541) was added at an 1:50 stock:digest, and samples were incubated overnight in the presence of 2% acetonitrile (v/v) to initiate digestion. After overnight digestion, samples were diluted with 200 mM EPPS buffer to reduce the urea concentration to 1 M, maintaining 2% acetonitrile. Trypsin (Promega, Cat. No. V5113) was then added at a 1:100 stock:digest, and digestion continued for 6 hours at 37°C. Digestion efficiency was evaluated by LC-MS/MS analysis of 1 µL aliquots, with missed cleavage rates consistently below 10%.  TMT labeling and peptide fractionation  For each sample, 100 µg of solubilized proteins was subjected to TMTpro 18plex labeling. To initiate labeling, 30 μL of acetonitrile was added to each peptide solution, followed by the addition of TMTpro 18plex reagents (Thermo Fisher Scientific, Cat. No. A52045). The reaction mixtures were incubated at room temperature for 1 hour with occasional vortexing to ensure complete mixing. To assess labeling efficiency, 1 μL aliquots from each reaction were pooled and analyzed by LC-MS/MS. All samples showed >95% labeling efficiency. Reactions were quenched with hydroxylamine (50% aqueous solution) to a final concentration of 0.5% (v/v) and incubated for 15 minutes at room temperature and LC-MS/MS analysis was performed to assess peptide ratios. Based on this analysis, protein inputs were normalized across channels to ensure approximately equal loading.  The samples were then acidified with formic acid to pH < 3.0, and trifluoroacetic acid (TFA) was added to a final concentration of 0.1%. Labeled samples were pooled into a single multiplex and peptides were dried to 30% volume using vacuum centrifugation and subsequently reconstituted in 1% formic acid containing 0.1% trifluoroacetic acid (TFA). Reversed-phase solid-phase extraction (SPE) was performed using 200 mg Sep-Pak C18 cartridges (Waters, Cat. No. WAT054945). Cartridges were pre-conditioned sequentially with methanol, acetonitrile, and 1% formic acid with 0.1% TFA. Following sample loading, peptides were washed with three column volumes of 1% formic acid and eluted with 95% acetonitrile in 1% formic acid. A second multiplex was generated from the remaining unlabeled peptide material and processed in parallel for phosphopeptide enrichment. Peptides were first desalted using 500 mg Sep-Pak tC18 Vac RC solid-phase extraction (SPE) cartridges (Waters), followed by enrichment of phosphopeptides using the Pierce High-Select Fe-NTA Phosphopeptide Enrichment Kit (Thermo Scientific, Cat. No. A32992), with 200 μL of Fe-NTA slurry used per column per sample. Enrichment was performed according to the manufacturer’s instructions. The resulting phosphopeptides were analyzed by LC-MS/MS to assess enrichment efficiency for individual samples. Following validation, enriched phosphopeptides were labeled with TMT using the same protocol described above. Labeled phosphopeptide samples were then pooled, dried using a SpeedVac concentrator, and re-purified using Sep-Pak SPE prior to fractionation. For deep proteomic analysis, TMT-labeled samples (including both peptides and phosphopeptides) were fractionated by high-pH reversed-phase high-performance liquid chromatography (HPLC) on an Agilent 1260 Infinity II series. Separation was achieved using a gradient of increasing acetonitrile in 10 mM ammonium bicarbonate (pH ~8.0). Eluted fractions were collected into 96 wells and concatenated into 24 pooled fractions for downstream LC-MS/MS analysis."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Mass spectrometry analysis Peptides were analyzed using a Vanquish Neo nano-ultra-high-performance liquid chromatography (nano-UHPLC) system (Thermo Fisher Scientific) coupled to a 25 cm × 75 µm internal diameter, 1.7 µm C18 Aurora Ultimate capillary column (IonOpticks), maintained at 60 °C. Peptide separation was carried out at a flow rate of 500 nL/min over a 240-minute linear gradient from 5% to 100% Buffer B (95% acetonitrile, 0.1% formic acid), with Buffer A composed of 0.1% formic acid in water. Quantitative mass spectrometry analysis was described recently77Eluted peptides were analyzed on an Orbitrap Ascend Tribrid mass spectrometer (Thermo Fisher Scientific) using a tandem mass tag (TMT)-based MS2 acquisition method coupled with high-field asymmetric waveform ion mobility spectrometry (FAIMS) at compensation voltages of –40 V, –60 V, and –80 V. Full MS (MS1) scans were acquired in the Orbitrap at a resolution of 120,000. MS2 scans were obtained at a resolution of 30,000 following higher-energy collisional dissociation (HCD) with a normalized collision energy of 33%. The quadrupole isolation window was set to 0.7 m/z. Maximum injection times were 100 ms for MS1 and ranged from 59 to 400 ms for MS2. Raw MS data were searched using the COMET search engine 78against the human UniProt reference proteome (downloaded April 19, 2024). Static modifications included +304.207145 Da on peptide N-termini and lysine residues (TMT), and +57.021464 Da on cysteine residues (carbamidomethylation). Oxidation of methionine (+15.994914 Da) and phosphorylation of serine, threonine, and tyrosine residues (+79.966330 Da) were considered as dynamic modifications. Peptide-spectrum matches (PSMs) were filtered to a false discovery rate (FDR) below 1% at both the peptide and protein levels using a target-decoy approach followed by linear discriminant analysis (LDA). Quantified peptides required a summed TMT signal-to-noise (S/N) ratio greater than 200 and an isolation specificity of at least 70%.  Fold changes across pairs of conditions (PTX vs DMSO, PTX+JNK-IN-8 vs PTX, and PTX+GNE-495 vs PTX) and FDR-adjusted p-values (Benjamini-Hochberg method) were calculated for each protein using limma package (Version 3.64.1) in R (Version 4.5.1), following log2 transformation of protein intensity values. For phosphoprotein abundance data, an additional normalization step was applied to account for the corresponding protein abundance by subtracting log2-transformed protein levels, thereby isolating phosphorylation-specific changes independent of overall protein expression. Differentially abundant protein and phosphoprotein lists were filtered based on adjusted p-values (FDR ≤ 0.05). Enrichment analysis was performed against gene sets from Gene Ontology biological processes using the gseapy package (Version 1.1.4). Enrichment was calculated separately for upregulated and downregulated protein sets to capture direction-specific biological processes and pathways."],"omics_type":["Proteomics"],"labhead":["Clifford Woolf"],"instrument_platform":[""],"labhead_affiliation":["Department of Neurobiology, Harvard Medical School; Boston, USA."],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["mkalocsay@mdanderson.org"],"submitter_affiliation":["The University of Texas MD Anderson Cancer Center\nDepartment of Experimental Radiation Oncology"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"A human iPSC-derived sensory neuron platform for high-throughput discovery of neuroprotectants against chemotherapy-induced peripheral neuropathy","description":"Chemotherapy-induced peripheral neuropathy (CIPN) is a major dose-limiting side effect of cancer treatment, yet the lack of predictive human models has hindered therapeutic progress. We have established a scalable model of paclitaxel-induced axon degeneration and neurotoxicity in iPSC-derived sensory neurons, suitable for high-throughput discovery of neuroprotective compounds. Using this platform, we screened 192 kinase inhibitors and identified 19 hits that commonly inhibited three STE20 kinases - MAP4K4, MINK1, and TNIK. Genetic knockdown revealed that multi-kinase inhibition of STE20 kinases is required for neuroprotection against paclitaxel. Moreover, selective pharmacological inhibition of STE20 kinases rescued paclitaxel-induced axon degeneration in iPSC-derived sensory neurons and primary human DRG, as well as preserved intraepidermal nerve fiber density in a mouse model of CIPN. These results establish a translational human sensory neuron platform for target and drug discovery in CIPN.","dates":{"publication":"2026-04-03","submission":"2026-02-26"},"accession":"PXD074954","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:7719","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:8247","NEWT:986","NEWT:52641","NEWT:28532","NEWT:35315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