{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069264/EX1_02142025_P00019_Anthony_Kossiakoff_APEX_1_S1_Proteins.xlsx"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069264/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069264/EX1_02142025_P00019_Anthony_Kossiakoff_PK_1_S9.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069264/EX1_02142025_P00019_Anthony_Kossiakoff_PK_4_S12.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069264/EX1_02142025_P00019_Anthony_Kossiakoff_PK_2_S10.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069264/EX1_02142025_P00019_Anthony_Kossiakoff_PK_3_S11.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069264/EX1_02142025_P00019_Anthony_Kossiakoff_APEX_2_S2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069264/EX1_02142025_P00019_Anthony_Kossiakoff_APEX_1_S1.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069264/EX1_02142025_P00019_Anthony_Kossiakoff_APEX_3_S3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/03/PXD069264/EX1_02142025_P00019_Anthony_Kossiakoff_APEX_4_S4.raw"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["koss@bsd.uchicago.edu"],"submitter":["Tomasz  Slezak"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Cell surface proteome","Inside-out proteins","Tumor-specific biomarkers"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069264"],"tissue":["Cell Culture"],"sample_protocol":["HCT116 cells were cultured to ~90% confluency. Following trypsinization and two phosphate buffered saline (PBS) washes, cells (6 × 10⁶ per replicate) were resuspended in 1 mL 200 nM APEX2 solution. After the addition of 1 mL substrate solution (50 mM biotin-PEG4-phenol, 0.1% H₂O₂ in PBS) and incubation for 60 seconds, 1 mL quencher solution (50 mM NaN₃, 100 mM sodium ascorbate, 50 mM Trolox in PBS) was added. Cells were washed twice in PBS, then incubated with 50 mM Proteinase K (Invitrogen) in reaction buffer (50 mM Tris-HCl, 7.5 mM CaCl₂, pH 7.5; 1 mL per 4 × 10⁶ cells) or reaction buffer alone (control) for 1 hour on ice with occasional mixing. Subsequent washes in reaction buffer removed the enzyme. Mass Spectrometry Cells were lysed in 400 µL RIPA buffer (Millipore Sigma) on ice for 30 minutes with occasional mixing. Lysates were clarified by centrifugation, and protein concentrations were determined using the Bradford assay (Thermo Scientific). For each sample, 250 µg lysate was applied to columns containing 400 µL NeutrAvidin Agarose Resin (Thermo Scientific), equilibrated in RIPA. Following a 3-hour incubation at 4°C with rotation, columns were washed with 10 mL each of RIPA, PBS/1M NaCl, and 50 mM NH₄HCO₃/2 M urea. Columns were subjected to on-resin reduction and alkylation with 100 µL LYSE solution (iST Sample Preparation Kit, PreOmics) at 55°C, 1000 rpm for 10 minutes, followed by digestion with 50 µL DIGESTION solution at 37°C, 500 rpm for 90 minutes. Supernatants were collected, 100 µL STOP solution added, and samples desalted and eluted per PreOmics protocol. Peptides were vacuum-dried and resuspended in LC-LOAD solution for LC-MS/MS. Mass spectrometry was performed on an Exploris 480 (Thermo Scientific) coupled to an UltiMate 3000 nanoLC system. Peptides were separated on a 50 cm MonoCap column (0.75 mm ID, GL Sciences) at 500 nL/min, 25°C, with the following solvent B (0.1% formic acid in acetonitrile) gradient: 0–5 min: 5%; 5–105 min: 22%; 105–124 min: 34%; 124–125 min: 95%; 125–130 min: 95%; 130–131 min: 4%; 131–145 min: 4%. Full scan MS spectra were acquired from m/z 350–1200 at 120,000 resolution, 50 ms maximum injection time, and AGC target 3e6. The cycle time was 3 s; the intensity threshold was 5e4. MS/MS scans used 15,000 resolution, 40 ms maximum injection time, AGC target 4e4, isolation window 1.6 m/z, first mass 110 m/z, and NCE 30. Dynamic exclusion was set to 30 seconds and charge states 2–7 were analyzed."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Raw data were analyzed using Proteome Discoverer v3.0.0.757 (ThermoFisher), searching against the human protein database with the Sequest HT engine. Mass tolerances were set to 10 ppm (precursor) and 0.02 Da (fragment). Peptides were filtered at a 1% FDR using the Target Decoy PSM Validator. Trypsin was specified as the protease (full specificity; up to three missed cleavages; minimum peptide length 7 aa, maximum 35 aa). Fixed modification: carbamidomethylation (+57.021 Da, cysteine); dynamic modifications: oxidation (+15.995 Da, methionine), protein N-terminal methionine loss (−131.040 Da), N-terminal acetylation (+42.011 Da), N-terminal methionine loss with acetylation (−89.030 Da). Protein abundance tables were exported to Perseus (v2.1.1.0, MaxQuant) (1). Statistical significance was determined using two-sample t-tests. Protein abundance fold changes were calculated as the ratio of the median abundance in non-proteinase K-treated cells to that in treated cells. Enrichment and network analyses were performed with STRING v12.0 and Cytoscape v3.10.2 (2, 3). Visualizations were generated in GraphPad Prism and Origin 2025 v10.2.0.196."],"omics_type":["Proteomics"],"labhead":["Anthony A Kossiakoff"],"instrument_platform":[""],"labhead_affiliation":["Department of Biochemistry and Molecular Biology, The University of Chicago, Chicago, IL 60637  Institute for Biophysical Dynamics, The University of Chicago, Chicago, IL 60637."],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["slezak@uchicago.edu"],"submitter_affiliation":["University of Chicago"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Dynamic translocation of Inside-Out proteins to the cell surface underlies cellular adaptation to cancer-induced stress.","description":"Inside-out (I-O) protein display, the non-canonical surface localization of intracellular proteins, represents an underexplored feature of tumor cell biology. Here, we map the molecular landscape and trafficking mechanisms that control the presentation of I-O proteins on cancer cell membranes. Employing APEX2-mediated proximity biotinylation and a custom antibody generation and validation platform, we identified approximately 140 high-confidence I-O proteins, primarily ribosomal, proteasomal, chaperone, and translation factors, notably enriched in protein families associated with stress-response pathways. Validation of 500 antibodies encompassing 40 I-O targets across seven tumor cell lines confirmed selective and robust surface localization, while in vivo imaging in mouse xenografts demonstrated pronounced and tumor-specific antibody accumulation. I-O proteins were absent on PBMCs and in normal tissues, indicating cancer cell selectivity. Functional analyses revealed that I-O protein tethering to the membrane is dependent on heparan sulfate interactions; enzymatic removal of these glycans led to the clearance of I-O proteins from the cell surface. Notably, the removed proteins returned to baseline levels within six hours, indicating a dynamic balance related to ER-Golgi trafficking and cellular stress. Nearly half of these I-O proteins overlapped with known stress granule components; however, stress elements that promote stress granule formation do not similarly affect surface display of I-O proteins. Furthermore, I-O proteins are present on standard cancer cell lines under lower stress levels needed to induce stress granule formation, suggesting parallel yet mechanistically distinct aspects of the stress response. These findings position I-O display as a new paradigm in protein trafficking, different from traditional secretion pathways and closely linked to stress 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