{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/03_28_25_Rupa_31_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/03_28_25_Rupa_21_1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/03_28_25_Rupa_21_2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/03_28_25_Rupa_31_2.raw"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/03_28_25_Rupa_21_1.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/03_28_25_Rupa_21_2.mzid_03_28_25_Rupa_21_2.MGF","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/03_28_25_Rupa_31_1.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/03_28_25_Rupa_31_2.mzid_03_28_25_Rupa_31_2.MGF","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/03_28_25_Rupa_31_1.mzid_03_28_25_Rupa_31_1.MGF","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/03_28_25_Rupa_21_2.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/03_28_25_Rupa_31_2.mzid","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/05/PXD069327/03_28_25_Rupa_21_1.mzid_03_28_25_Rupa_21_1.MGF"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["p.rao@duke.edu"],"submitter":["Nik Skiba"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"disease":["Disease Free"],"software":[""],"submitter_keywords":["Human","Cytoskeleton","Proteome","Lens"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069327"],"tissue":["Brain","Fibroblast"],"sample_protocol":["Extraction of cytoskeletal-enriched fraction: Intact frozen lenses derived from 21- and 31-year-old donors were initially thawed on ice and the lens epithelium was removed using fine forceps under a dissecting microscope. The rest of the lens mass composed of fibers was used for  extraction of the cytoskeletal fraction as described by Cho et.al.,26 with a minor modification.   Briefly,  lenses without a capsule were weighed and rinsed twice with ice-cold phosphate-buffered saline (PBS, pH 7.4), then homogenized gently on ice using a Dounce glass homogenizer in freshly prepared ice-cold cell lysis buffer (wt/vol, 100 mg/ml) containing: 50 mM PIPES (piperazine-N,N′-bis), 50 mM NaCl, 5% glycerol, 0.1% NP-40, 0.1% Triton X-100, 0.1% Tween-20, 5 mM sodium fluoride, 2 mM sodium orthovanadate, and protease and phosphatase inhibitors (protease inhibitor tablet, 11836170001; PhosStop tablet, 04906837001, Millipore Sigma). Homogenization was performed gently with 10 upward and 10 downward strokes. The homogenates were transferred into Eppendorf tubes, placed on a rotating rocker, and incubated for 10 min at 4 °C. They were then centrifuged at 10,000 × g for 10 min at 4 °C. The supernatants, labeled as the cytosolic fraction, were collected, kept on ice, and reserved for later steps. The pellets were disrupted gently using a blue pestle (Axygen, PES-15-B-SI, Corning Incorporated), rinsed twice with ice-cold 50 mM Tris-HCl buffer (pH 7.5), and incubated at room temperature for 15 min in nuclease buffer containing 50 mM Tris–HCl (pH 7.5), 10 mM MgCl₂, 2 mM CaCl₂, and 10 U/ml Benzonase nuclease (Millipore Sigma). The nuclease buffer was removed by centrifugation of the samples at 10,000xg for 10 min at 4 oC, and the previously collected cytosolic lysate was added back to the respective pellets, disrupted with blue pestle and incubated on ice for an additional 5 min to release and solubilize DNA/RNA-binding proteins. The supernatants were then collected back into the tubes as cytosolic fraction after centrifugation.  The pellets were rinsed three more times with ice-cold Tris-HCl buffer. Finally, the pellets, representing the cytoskeletal-enriched fraction, were resuspended in 500 µl of 1% sodium dodecyl sulfate (SDS) in low-binding Eppendorf tubes. Protein was quantified using a BCA (bicinchoninic acid) assay kit, and the samples were further processed for proteomic analysis.27 All rinsing/washing steps were carried out by centrifugation at 10,000 × g for 10 min at 4 oC, and pellets were disrupted as needed with a blue plastic pestle."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Mass spectrometry: Samples were solubilized in 100 mM Tris-HCl (pH 8.0) containing 2% sodium dodecyl sulfate, reduced with 10 mM DTT, alkylated with 25 mM iodoacetamide, and subjected to tryptic hydrolysis using the HILIC beads SP3 protocol as previously described.28 The protein digests were separated on EasySpray PepMap Neo 75 m X 150 mm, 2 m, C18 column (Thermo Scientific) over 90 min at a flow rate of 0.3 μl/min at 35°C using Vanquish Neo UHPLC system (Thermo Scientific). The 5-30% mobile phase B gradient was used, where phase A was 0.1% formic acid in water and phase B 0.1% formic acid in 80% acetonitrile. Peptides separated by liquid chromatography (LC) were introduced into the Q Exactive HF Orbitrap LC-MS-MS mass spectrometer (Thermo Scientific) using positive electrospray ionization at 1900 V and capillary temperature of 275°C. Data collection was performed in the data-dependent acquisition (DDA) mode with 120,000 resolution (at m/z 200) for MS1 precursor measurements. The MS1 analysis utilized a scan from 375-1500 m/z with a target AGC value of 1.0e6 ions, the RF lens set at 30%, and a maximum injection time of 50 ms. Advanced peak detection and internal calibration (EIC) were enabled during data acquisition. Peptides were selected for MS/MS using charge state filtering, monoisotopic peak detection and a dynamic exclusion time of 20 sec with a mass tolerance of 10 ppm. MS/MS was performed using HCD (High-Energy Collisional Dissociation) with a collision energy of 30±5% with detection in the ion trap using a rapid scanning rate.  For protein identification and quantification, raw mass spectral data files (.raw) were imported into Scaffold 5 (Proteome Software). Peptides were identified using Mascot version 2.5.2 (Matrix Science) for searching the UniProt 2023 reviewed human database containing 20,237 entrees. Mascot search parameters were: 10 ppm mass tolerance for precursor ions; 0.025 Da for fragment-ion mass tolerance; one missed cleavage by trypsin; fixed modification was carbamidomethylation of cysteine; variable modifications were oxidized methionine and deamination of asparagine and glutamine. Only proteins identified with 2 or more peptides (FDR < 1%), were included in the protein quantification analysis. Values representing protein amounts were calculated based on an emPAI (Scaffold 5) algorithm utilizing spectral counting"],"omics_type":["Proteomics"],"labhead":["Ponugoti V. Rao"],"instrument_platform":[""],"labhead_affiliation":["Duke University Eye Center"],"submission_type":["COMPLETE"],"species":["Homo Sapiens (human)"],"submitter_mail":["skibanik@gmail.com"],"publication":["42149027 Maddala R, Lankford LK, Skiba NP, Rao PV. The Human Lens Fiber Cytoskeletome Reveals Neuronal Signatures and the Presence of Chaperonins, Proteasome, Signaling, and Redox Regulators. Invest Ophthalmol Vis Sci. 2026 67(5):45 10.1167/iovs.67.5.45"],"submitter_affiliation":["Duke University"],"submitter_country":["United States"],"doi":["10.6019/PXD069327"],"pubmed_abstract":["<h4>Purpose</h4>Morphogenesis, growth, shape, mechanics, and transparency of the ocular lens critically depend on cytoskeletal networks and cell adhesive interactions. However, the molecular composition of these cellular components of lens fibers remains to be defined in depth. This study is aimed at providing an unbiased and comprehensive characterization of cytoskeletal and cytoskeleton-associated proteins in human lens fibers.<h4>Methods</h4>Transparent lenses from young adult human donors (ages 21 and 31), with capsules removed, were processed to enrich the cytoskeletome fraction, which was then trypsin-digested and subjected to proteomics analysis using a Q Exactive HF Orbitrap LC-MS/MS spectrometer. Selected proteins were validated by immunoblotting and immunofluorescence. Gene Ontology enrichment analysis was performed to classify the identified proteins.<h4>Results</h4>Proteomic analysis identified 530 proteins in the human lens fiber cytoskeletome, including known and lesser-known cytoskeletal, membrane-associated, adhesive, scaffolding, signaling, and metabolic proteins. Notably, several neuron preferred proteins, chaperonins, and proteasome, signaling, and redox regulators were enriched in the cytoskeletal interactome. Many of the neuron preferred proteins were localized to the cortical lens fiber cells. In addition, certain cytoskeletal protein profiles differed between human and mouse lenses.<h4>Conclusions</h4>This study provides the first comprehensive profile of the human lens fiber cytoskeletome. It highlights the presence of neuron-enriched cytoskeletal, adhesive, and scaffolding proteins; cytoskeletal chaperonins; proteasome, signaling, and redox regulators; and both canonical and lesser-known cytoskeletal proteins. These findings suggest that a diverse, complex, and dynamically regulated cytoskeletal network contributes to lens fiber cell architecture, adhesion, trafficking, mechanics, and clarity."],"pubmed_title":["The Human Lens Fiber Cytoskeletome Reveals Neuronal Signatures and the Presence of Chaperonins, Proteasome, Signaling, and Redox Regulators."],"pubmed_authors":["Maddala Rupalatha R, Lankford Levi K LK, Skiba Nikolai P NP, Rao Ponugoti V PV"],"additional_accession":[]},"is_claimable":false,"name":"The Human Lens Fiber Cytoskeletome Reveals Neuronal Signatures, and the presence of Chaperonins, Signaling, Proteasome and Redox Regulators","description":"Morphogenesis, growth, shape, mechanics, and transparency of the ocular lens critically depend on cytoskeletal networks and cell adhesive interactions. However, the molecular composition of these cellular components of lens fibers remains to be defined in depth. This study is aimed at  providing an unbiased and comprehensive characterization of cytoskeletal and cytoskeleton-associated proteins in human lens 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