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Canbay"],"technology_type":["Mass Spectrometry","Data-independent acquisition","Bottom-up proteomics"],"disease":["Wounds And Injuries"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD050151"],"tissue":["Epithelial Cell","Keratinocyte","Skin"],"sample_protocol":["Protein concentration was determined by BCA assay and adjusted protein lysates were stored at -80 °C. Lysates were reduced with DTT, alkylated by iodoacetamide, and digested with Lys-C. After dilution, they were further digested overnight with trypsin. Protease activity was quenched by acidification with TFA and peptides were purified by SPE using HR-X columns and C18 cartridges. The peptides were frozen in liquid nitrogen and lyophilized prior to phosphopeptide enrichment.  The enrichment of phosphopeptides was executed automatically through a Bravo Automated Liquid Handling Platform. Fe (III)-NTA cartridges were primed with TFA in acetonitrile and then balanced with TFA in acetonitrile. Peptides were redissolved in equilibration buffer and loaded onto the cartridges. Phosphopeptides were extracted with ammonia in acetonitrile into formic acid. These samples were then concentrated via a lyophilizer and reconstituted in formic acid for subsequent LC-MS/MS analysis.  HRMS1-DIA proteome data sets were acquired at the DTU Proteomics Core. For each resuspended keratinocyte proteome, peptides were analysed using the preset method on the EvoSep One instrument. Peptides were eluted over a defined gradient and analysed by mass spectrometry, Orbitrap Exploris 480. Full MS spectra were collected and the MS2 spectra were obtained in DIA mode in the Orbitrap. Each DIA experiment covered a range of 200 m/z resulting in three DIA experiments. Between the DIA experiments a full MS scan is performed. MS performance was verified for consistency by running complex cell lysate quality control standards, and chromatography was monitored to check for reproducibility. HRMS1-DIA phosphoproteomics data sets were acquired at the MAPP at University of Fribourg. Each enriched keratinocyte phosphoproteome was analysed with an Easy-nLC 1200 coupled to an Orbitrap Exploris 480 mass spectrometer operated with a DIA method. Peptides were separated on a fused silica HPLC-column tip using a gradient of mobile phase A and B. The column temperature was maintained at 50 °C. The total gradient time was 140 min. Flow rate was kept at 250 nL/min. Re-equilibration was done prior to sample pickup and loading. Spray voltage was set to 1.9 kV, funnel RF level at 40, and heated capillary at 275 ◦C. Full MS spectra were collected at a resolution of 120000. The MS2 spectra were obtained in DIA mode in the Orbitrap operating at a resolution of 60000. Each DIA experiment covered a range of 200 m/z resulting in three DIA experiments. Between the DIA experiments, a full MS scan was performed. All data were acquired in profile mode using positive polarity. MS performance was verified for consistency by running complex cell lysate quality control standards, and chromatography was monitored to check for reproducibility."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Two independent searches for the proteome and phosphopeptide samples were performed. For the proteome, raw files were analysed using Spectronaut™ (Biognosys, Schlieren, Switzerland, version 18.5) directDIA+ (deep) default settings, spectra were matched against the homo sapiens reference FASTA database (UP000005640; downloaded from Uniprot on 27th of December 2022). Dynamic modifications were set as Oxidation (M) and Acetyl on protein N- termini. Cysteine carbamidomethyl was set as a static modification. Protein quantitation was done on the MS1 level, data filtering set to Q-value and the data was normalized by RT-dependent local regression model and protein groups were inferred by IDPicker. For phosphopeptides, raw files were analysed using Spectronaut™ (Biognosys, version 18.5) directDIA+ (deep), spectra were matched against the homo sapiens database (UP000005640; downloaded from Uniprot on 27th of December 2022) with the BGS Phospho PTM workflow with the following modifications: deamidation (NQ) and oxidation (M) were added as dynamic modifications together with Phospho (STY) and Acetyl on protein N-termini. Cysteine carbamidomethyl was set as a static modification. All results were filtered to a 1% FDR, data filtering set to Q-value and protein quantitation done on the MS1 level. The data was cross-normalized by a RT-dependent local regression model on modified (phospho)-peptides. The PTM probability cutoff was set to 0."],"omics_type":["Proteomics"],"labhead":["Chiara Francavilla"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Section for Protein Science and Biotherapeutics, Department of Biotechnology and Biomedicine, Technical University of Denmark, Søltofts Plads, 2800, Kongens Lyngby, Denmark"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["vahcan@dtu.dk"],"submitter_affiliation":["Technical University of Denmark"],"submitter_country":["Denmark"],"additional_accession":[]},"is_claimable":false,"name":"Mulit-omics analysis of keratinocytes reveals dermokine as regulator keratinocyte differentiation and adhesion - phosphoproteome and proteome","description":"Impaired adhesion and differentiation of keratinocytes is a hallmark of several skin diseases, but only some of the factors that regulate these processes have been identified. Here, we studied the role of isoform-rich dermokine – a wound- and tumor-regulated protein – in keratinocytes using a combination of multi-omics and functional approaches. CRISPR/Cas9-induced knockout of dermokine isoforms in human keratinocytes inhibited differentiation of these cells in three-dimensional organotypic skin cultures, which was confirmed by quantitative proteomics. In two-dimensional monocultures, dermokine deficiency affected the proteome and phosphoproteome as revealed by mass spectrometry. We found reduced abundance of differentiation-specific proteins and increased phosphorylation of cell adhesion protein p120 (catenin-δ1). The adhesive strength of dermokine knockout keratinocytes was impaired, which was rescued by p120 knock-down or ROCK inhibition. Finally, we verified the correlation between decreased dermokine expression and increased p120 phosphorylation in human non-healing wounds. These results identify dermokine as regulator of keratinocyte adhesion and differentiation, involving at least in part its effect on p120 phosphorylation and ROCK. Our data point to a function of dermokine in the pathogenesis of chronic wounds.","dates":{"publication":"2026-04-09","submission":"2024-02-26"},"accession":"PXD050151","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:108018","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:1126","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:1367493","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:46429","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:2736291","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","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:656061","NEWT:37965","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:2767846","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:468822","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","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:342808","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:99802","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:709964","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:156974","NEWT:3714","NCBITaxon:37162","NEWT:3715","NEWT:2065263","NEWT:199225","NEWT:1549675","NEWT:177437","NEWT:717966","NEWT:9014","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:29022","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:96795","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:1883426","NEWT:8165","NEWT:96794","NEWT:10401","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:215451","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:485","NEWT:329032","NEWT:56636","NEWT:2499525","NEWT:55307","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:2830","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:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:141469","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:1578","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:291146","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:1092586","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:911022","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:717989","NEWT:33952","NEWT:1255232","NEWT:11723","NEWT:445","NEWT:153009","NEWT:1004879","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:156981","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:2729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