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Cells were lysed in lysis buffer (8M urea, 200 mM EPPS pH 8.5, and protease inhibitors (Pierce, A32953)) and homogenized by passing through a 20G needle. Protein was quantified by BCA followed by disulfide bond reduction with 5 mM Pierce neutralized TCEP for 15 min at room temperature protected from light. Alkylation with 10 mM iodoacetamide was performed by incubating at room temperature for 30 minutes protected from light before the reaction was quenched with 5 mM DTT. 100 ug of protein was collected for chloroform-methanol precipitation and resuspended in EPPS buffer (200 mM, pH 8.5). Samples were digested at a 1:100 enzyme-to-protein ratio with LysC protease at room temperature overnight. Samples were then digested again at a 1:100 enzyme-to-protein with trypsin for 6 hours at 37°C.  Approximately 50 ug of peptides from each sample was labelled with 100 ug TMT reagent which were dissolved in anhydrous ACN to achieve a final concentration of 30\\% (v/v). TMT-labelled samples were acidified, vacuum centrifuged to near dryness and subjected to C18 SPE (Sep-Pak, Waters). Samples were subjected to basic pH reversed-phase HPLC. Offline fractionation was performed using an Agilent 1200 pump with an Agilent 300Extend C18 column (3.5 μm particles, 2.1 mm ID and 250 mm in length). Peptides were subjected to a 50 min linear gradient from 5% to 35% acetonitrile in 10 mM ammonium bicarbonate pH 8 at a column flow rate of 0.25 mL/min. Ninety-six fractions were collected and then concatenated into 24, of which 12 non-adjacent samples were analyzed."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Database searching included all human entries from UniProt. The database was concatenated with one composed of all protein sequences in the reversed order. Sequences of common contaminant proteins were also included. Searches were performed using a 50-ppm precursor ion tolerance and 0.03 Da product ion tolerance. TMTpro on lysine residues and peptide N termini (+304.2071 Da) and carbamidomethylation of cysteine residues (+57.0215 Da) were set as static modifications (except when testing for labeling efficiency, when the TMTpro modifications were set to variable), while oxidation of methionine residues (+15.9949 Da) was set as a variable modification.  Peptide spectrum matches (PSMs) were adjusted to a 1\\% false discovery rate (FDR) (Mirzaei, Gupta et al. 2017). PSM filtering was performed using linear discriminant analysis (LDA) as described previously (Mirzaei, Gupta et al. 2017), while considering the following parameters: XCorr, ΔCn, missed cleavages, peptide length, charge state, and precursor mass accuracy. Protein-level FDR was subsequently set at 1%. For reporter ion quantification, a 0.003 Da window around the theoretical m/z of each reporter ion was scanned, and the most intense m/z was used. Peptides were filtered to include only those with a summed signal-to-noise ratio ≥100 across all channels. For each protein, the filtered signal-to-noise values were summed to generate protein quantification values. To control for different total protein loading within an experiment, the summed protein quantities of each channel were adjusted to be equal in the experiment."],"omics_type":["Proteomics"],"labhead":["James A DeCaprio"],"instrument_platform":[""],"labhead_affiliation":["Dana-Farber Cancer Institute Department of Medical Oncology  Harvard Medical School Boston, MA USA"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["Not available"],"submitter_mail":["joao_paulo@post.harvard.edu"],"submitter_affiliation":["Harvard Medical School"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"PRMT5 regulates splicing of detained introns from DNA damage repair genes to protect against replication stress","description":"Protein arginine methyltransferase 5 (PRMT5) catalyzes the formation of symmetric dimethyl arginine on a broad range of cellular targets, and PRMT5 inhibitors (PRMT5i) show drastic anti-proliferative effects in preclinical studies. Several models have been proposed to explain and predict sensitivity to PRMT5 inhibition including through p53 activation and DNA damage response regulation. Here, we interrogate the underlying mechanisms of PRMT5i sensitivity in Merkel cell carcinoma, a high-grade neuroendocrine carcinoma of the skin that is that is highly sensitive to p53 activation. We observed that although PRMT5 inhibition activated p53, p53 loss did not impact PRMT5i sensitivity. To identify critical pathways altered by PRMT5i, we conducted a genome-wide CRISPR/Cas9 screen and found that PRMT5i-treated cells have an increased dependency on splicing factors. Furthermore, proteomic analysis found that levels of mRNA splicing factors increased after PRMT5i treatment. Characterization of the transcriptome revealed a disruption in mRNA splicing of detained introns in both PRMT5i sensitive and resistant lines. We observed that basal levels of detained introns correlated with PRMT5 inhibitor sensitivity, and that PRMT5 was required to maintain genome integrity through ATR/CHK1 signaling. Our findings support a threshold model of genome stability, in which cells can tolerate an increase in detained introns until a point where DNA damage pathways are triggered, and cells undergo apoptosis. ","dates":{"publication":"2026-06-19","submission":"2025-04-11"},"accession":"PXD062850","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","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:1073882","NEWT:6819","NEWT:475174","NEWT:111205","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","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:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:111225","NEWT:7719","NEWT:5530","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:49928","NEWT:3349","NEWT:160621","NEWT:212790","NEWT:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","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:2579791","NEWT:44685","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:2065263","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:321967","NEWT:320637","NEWT:1078283","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:415978","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:33941","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:575412","NEWT:28112","NEWT:49012","NEWT:6493","NEWT:10832","NEWT:6494","NEWT:6491","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:643680","NEWT:214092","NCBITaxon:6157","NEWT:13095","NEWT:162425","NEWT:104105","NEWT:216257","NEWT:9986","NEWT:8654","N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