{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072104/Result.xlsx"],"Tabular":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072104/IdentifiedAndQuantifiedProteins.tsv"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072104/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072104/Neurons_PSP_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072104/Neurons_PSP_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072104/Neurons_PSP_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072104/Neurons_PSP_4.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD072104/SearchPSPvsHC.sne"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["gaspari@unicz.it"],"submitter":["Caterina Gabriele"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"disease":["Progressive Supranuclear Palsy"],"software":[""],"submitter_keywords":["neurofilament","dopaminergic neurons","Tauopathy; progressive supranuclear palsy; neurofilament; dopaminergic neurons; axonal degeneration; autophagy modulation","axonal degeneration","Tauopathy","autophagy modulation","progressive supranuclear palsy"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072104"],"tissue":["Dopaminergic Neuron","Cell Culture"],"sample_protocol":["Proteomic profiling was performed on four biological replicates each from pooled HC (pHC) and sPD (pPD) mDA neurons, previously lysed as described for Western blotting. Ten micrograms of proteins, after reduction and alkylation, were then processed by Protein Aggregation Capture (PAC). Briefly, 5 µL of MagResyn Hydroxyl beads (100 µg) were equilibrated with two washes in 70% acetonitrile (ACN). Protein binding was induced by adding ACN to 70% final concentration, followed by 10 min incubation at 1100 rpm. The beads were washed three times in ACN and once in 70% ethanol, then resuspended in 50 µL of 50 mM triethylammonium bicarbonate (TEAB). Proteins were digested overnight at 37 °C with 200 ng of Trypsin-LysC (Pierce, Thermo Fisher) at a 1:50 enzyme-to-substrate ratio. Peptides were collected and residual material eluted with 50 µL of 0.1% formic acid. Harvested peptides were injected for LC-MS/MS analysis without further purification.Peptides were analyzed by nanoLC-MS/MS using an Orbitrap Exploris 480 mass spectrometer coupled to an Easy-nLC 1200 system (Thermo Fisher). Peptides were loaded onto a 17 cm in-house packed silica capillary column (75 µm i.d., 3 µm C18; Dr. Maisch). Separation was achieved using a binary gradient of mobile phase A (2% ACN, 0.1% FA) and mobile phase B (80% ACN, 0.1% FA) at 300 nL/min over 140 min: 3–25% B over 90 min, 25–40% over 30 min, 40–100% over 8 min, followed by 10 min at 100% B. The column was re-equilibrated at 0% B for 2 min. Data were acquired using data-independent acquisition (DIA) mode. Full scans were acquired at a resolution of 60,000, followed by 30 DIA scans at a resolution of 30,000 with 5e5 AGC target, 50 ms maximum injection time, and 25% normalized collision energy. DIA isolation windows consisted of 23 × 15 m/z, 4 × 30 m/z, and 3 × 50 m/z segments (0.5 m/z overlap) covering 350–1010 m/z."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Raw files were analyzed with Spectronaut (v18.7) using the Human 1 Protein 1 Gene database (20,577 sequences, March 2022). Quantitative analysis was performed using Perseus (v2.0.11.0). Protein abundances were log2-transformed and filtered to include only proteins detected in ≥3 replicates per group. Differentially expressed proteins (DEPs) were identified via two-sample t-tests with permutation-based FDR correction (FDR < 0.05; S0 = 0.2).A total of 6,414 proteins were identified, of which 443 were differentially expressed between pPD and pHC mDAs (|log2FC| > 1.5; q < 0.05)."],"omics_type":["Proteomics"],"labhead":["Marco Gaspari"],"instrument_platform":[""],"labhead_affiliation":["Department of Experimental and Clinical Medicine, Magna Graecia University of Catanzaro, Catanzaro, 88100, Italy"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["cgabriele86@gmail.com"],"publication":["42121856 Covello R, Benedetto GL, Scalise S, Gabriele C, Valente D, Zannino C, Puccio B, Quattrone A, Guzzi PH, Gaspari M, Quattrone A, Cuda G, Parrotta EI. Cytoskeletal Imbalance and Axonal Vulnerability in Sporadic PSP-RS: Early Changes in a Human iPSC-Derived Neuronal Model with Altered mTOR Signaling. Cells. 2026 15(9):754 10.3390/cells15090754"],"submitter_affiliation":["Università Magna Graecia di Catanzaro"],"submitter_country":["Italy"],"pubmed_abstract":["Progressive supranuclear palsy-Richardson's syndrome (PSP-RS) is a primary 4R tauopathy in which early axonal dysfunction may precede overt neurodegeneration; however, the mechanisms linking Tau dysregulation to cytoskeletal vulnerability remain poorly defined. Here, we generated induced pluripotent stem cell (iPSC)-derived midbrain dopaminergic neurons from individuals with sporadic PSP-RS and matched healthy controls and performed integrated transcriptomic and proteomic analyses. PSP-RS neurons exhibited coordinated suppression of dopaminergic and synaptic programs alongside activation of cytoskeletal remodeling and stress-related pathways. These changes were accompanied by increased Tau phosphorylation, neurofilament accumulation, and structural alterations of the axonal compartment, consistent with an early axonopathic phenotype. Notably, mechanistic target of rapamycin (mTOR) signaling significantly increased. Pharmacological inhibition of mTOR reduced Tau phosphorylation and neurofilament levels, indicating that mTOR activity contributes to the maintenance of cytoskeletal imbalance. In conclusion, our findings support a model in which early cytoskeletal dysfunction in PSP-RS arises from the convergence of Tau dysregulation, impaired structural homeostasis, and altered signaling pathways. Rather than acting as a primary driver, mTOR appears to function as a pathogenic amplifier that sustains axonal stress. This study provides a human cellular framework to investigate early axonopathic mechanisms in sporadic PSP-RS."],"pubmed_title":["Cytoskeletal Imbalance and Axonal Vulnerability in Sporadic PSP-RS: Early Changes in a Human iPSC-Derived Neuronal Model with Altered mTOR Signaling."],"pubmed_authors":["Covello Raffaele R, Benedetto Giorgia Lucia GL, Scalise Stefania S, Gabriele Caterina C, Valente Desirèe D, Zannino Clara C, Puccio Barbara B, Quattrone Andrea A, Guzzi Pietro Hiram PH, Gaspari Marco M, Quattrone Aldo A, Cuda Giovanni G, Parrotta Elvira Immacolata EI"],"additional_accession":[]},"is_claimable":false,"name":"mTOR inhibition ameliorates tau burden and neurofilament pathology in sporadic PSP-RS neurons","description":"Progressive supranuclear palsy, Richardson’s syndrome subtype (PSP-RS), is a tauopathy marked by early axonal pathology and neurodegeneration. Modeling sporadic PSP-RS in human neurons remained a major challenge. Here, we generated midbrain dopaminergic (mDA) neurons from induced pluripotent stem cells (iPSCs) derived from idiopathic PSP-RS patients and healthy controls. Combined transcriptomic and proteomic analysis revealed reduced dopaminergic differentiation and synaptic function, alongside increased phosphorylated and oligomeric Tau, neurofilament accumulation, axonal swelling, and endoplasmic reticulum disorganization. These alterations coincided with impaired autophagic flux and elevated levels of phosphorylated mTOR. Pharmacological inhibition of mTOR restored autophagy and reduced neurofilament and tau pathology. Collectively, our findings implicate mTOR-dependent autophagy dysfunction as a key driver of early axonal pathology of PSP-RS and highlight autophagy modulation as a promising therapeutic 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