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MacDonald"],"software":[""],"tissue":["Brain"],"sample_protocol":["Total protein was extracted from the organoids by sonication. Lysate samples from two additional control cell lines were included to improve protein detection. A different randomized block was used for each stage of sample processing, TMT labeling, and mass spec analysis, balanced for genotype and timepoint. Total protein was estimated using microBCA assay and digested with trypsin on S-Traps (Protifi) per manufacture protocol. Samples were first assigned to one of five sets of TMTPro16 blocks (plex’s), such that each plex was balanced for genotype and timepoint, with a random order in each plex. Organoid samples from two additional, age-matched control cell lines with no isogenic pair were included within each plex to improve peptide diversity capture. These samples were later removed from downstream analyses. Reference controls for internal reference scaling (IRS) normalization were included within each plex. These reference controls were prepared by pooling equal amounts of lysate from all samples, which were digested separately, and then split in aliquots for TMT labeling. All TMT plex’s were labeled at the same time. For the reference control, peptides were reconstituted in 80 μl. A total of 40 μl was labeled with 12 μl TMTPro 134 N. All samples with in a plex were mixed along with 20 µg aliquots of each labeled pooled control, giving 320 µg total TMT labeled peptides per plex. Of this, 80 µg were used for peptide/protein quantification, and 240 µg was subject to phosphopeptide enrichment. Prior to peptide/protein quantification, the 80 µg aliquot was separated into 8 fraction using the Pierce High pH Reverse Phase Fractionation Kit per manufacturer protocol. For phosphopeptide enrichment, the 240 µg TMT-labeled peptide aliquot were desalted with C18 spin column. Phosphopeptides were enriched using the AssayMAP Agilent Bravo instrument with Fe(III)-NTA IMAC resin according to the manufacturer’s instructions. Peptides were resuspended in 210 µl 80% ACN 0.1% TFA, bath sonicated for 10 minutes, vortexed for 10 minutes, and quickly centrifuged. The resin was primed with 50% ACN 0.1% TFA and equilibrated with equilibration/wash buffer 80% ACN 0.1% TFA. Samples were loaded into the syringes then dispensed into the Flow Through Collection plate.Phosphopeptides were eluted in 18 µl 1% ammonium hydroxide solution and acidified with 1.8 µl 20% FA, and subject to high pH reverse phase fractionation as described above but condensed to 5 fractions."],"repository":["Pride"],"labhead":["Matthew MacDonald"],"instrument_platform":[""],"labhead_affiliation":["University of Pittsburgh Department of Psychiatry"],"submission_type":["COMPLETE"],"publication":["Not available"],"submitter_affiliation":["University of Pittsburgh"],"labhead_mail":["mlmacdonald@gmail.com"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Neurodevelopmental Disorder With Or Without Autism Or Seizures"],"submitter_keywords":["Pacs1","Brain organoids","Proteome","Neurodevelopmental disorders"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD080130"],"quantification_method":[""],"modification":[""],"data_protocol":["For peptide/protein quantification, TMT labeled peptides (~1 μg) were loaded onto a heated PepMap RSLC C18 2 μm, 100 angstrom, 75 μm x 50 cm column (Thermo Scientific) and eluted over 180 min gradients optimized for each high pH reverse-phase fraction (71). Sample eluate were electrosprayed (2000 V) into a Thermo Scientific Orbitrap Eclipse mass spectrometer for analysis. MS1 spectra were acquired at a resolving power of 120,000. MS2 spectra were acquired in the Ion Trap with CID (35%) in centroid mode. Real-time search (max search time = 34 s; max missed cleavages = 1; Xcorr = 1; dCn = 0.1; ppm = 5) were used to select ions for synchronous precursor selection for MS3. MS3 spectra were acquired in the Orbitrap with HCD (60%) with an isolation window = 0.7 m/z and a resolving power of 60,000, and a max injection time of 400ms. For phosphopeptide quantification, 4 μl (out of 20) of the TMT labeled phosphopeptide enrichments were loaded onto a heated PepMap RSLC C18 2 μm, 100 angstrom, 75 μm x 50 cm column (Thermo Scientific) and eluted over a 180 min gradient: 1 min 2% B, 5 min 5% B, 160 min 25% B, 180 min 35% B. Sample eluate was electrosprayed (2000 V) into a Thermo Scientific Orbitrap Eclipse mass spectrometer for analysis. MS1 spectra were acquired at a resolving power of 120,000. MS2 spectra were acquired in the Orbitrap with HCD (38%) in centroid mode with an isolation window = 0.4 m/z, a resolving power of 60,000, and a max injection time of 350 ms. The raw MS files were processed using Proteome Discoverer version 2.4 (Thermo Scientific, Waltham, MA). MS spectra were searched against the Homo sapiens Uniprot/SwissProt database. SEQUEST search engine was used (enzyme = trypsin, max. missed cleavage = 4, min. peptide length = 6, precursor tolerance = 10 ppm). Static modifications include carbamidomethyl (C, +57.021 Da) and TMT labeling (N-term and K, +304.207 Da for TMTpro16). Dynamic modifications include oxidation (M, +15.995 Da), Phosphorylation (S, T, Y,+79.966 Da, only for phosphopeptide dataset), acetylation (N-term,+ 42.011 Da), Met-loss (N-term, –131.040 Da), and Met-loss + Acetyl (N-term, –89.030 Da). PSMs were filtered by the Percolator node (max Delta Cn = 0y .05, target FDR (strict) = 0.01, and target FDR (relaxed)=0.05). Proteins were identified with a minimum of 1 unique peptide and protein-level combined q values < 0.05. Reporter ion quantification was based on corrected S/N values with the following settings: integration tolerance = 20 ppm, method = most confident centroid, co-isolation threshold = 70, and SPS mass matches = 65."],"omics_type":["Proteomics"],"species":["Homo Sapiens (human)"],"submitter_mail":["mlmacdonald@gmail.com"],"submitter_country":["United States"],"doi":["10.6019/PXD080130"],"additional_accession":[]},"is_claimable":false,"name":"PACS1 syndrome variant alters proteomic landscape of developing cortical organoids","description":"Several large-scale genetic studies investigating the cause of neurodevelopmental disorders (NDDs) have been conducted, leading to the identification of hundreds of risk genes. However, our understanding of the mechanisms by which the observed genetic variants act has lagged, limiting translation of genetic findings into clinical treatments. In recent years, patient-derived brain organoids have been increasingly used to model NDDs and identify pathogenic mechanisms. While most of these studies evaluate the mechanisms by which NDD risk genes and pathogenic variants affect the transcriptome, studies considering the proteome are limited. Here, we examine the effect of the pathogenic variant PACS1 p.R203W, causative of PACS1 Syndrome, on the proteomic landscape of brain organoids and compared it to our previously generated transcriptomic dataset. Although we observed low overlap between transcripts and proteins with altered expression and phosphorylation, most resulting dysregulated processes converged. The proteomic data not only reinforced the importance of these developmental processes for p.R203W pathogenesis, but also detected dysregulated processes not previously identified by the transcriptomic analysis. Key dysregulated transcripts and proteins observed in PACS1(+/R203W) organoids have been classified as NDD-causative and ASD-risk genes. Interestingly, the core neurodevelopmental features of PACS1 syndrome like intellectual disability, delayed speech, and epilepsy were enriched in all levels of regulation, while the facial and muscular abnormalities were enriched exclusively in the proteome and phosphoproteome. Our results highlight that proteomic analyses not only enhance our understanding of general NDD mechanisms by complementing transcriptomic studies, but also uncovering additional targets, and therefore facilitating therapy development.","dates":{"publication":"2026-08-07","submission":"2026-06-24"},"accession":"PXD080130","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:1073882","NEWT:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","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:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:44688","NEWT:44689","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:270643","NEWT:2065263","NEWT:177437","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:244366","NEWT:1246791","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:33548","NEWT:52299","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","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:373153","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","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:8655","NEWT:5147","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:80863","NEWT:90675","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:29829","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:231490","NEWT:244704","NEWT:7725","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:72664","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:45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