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Hendriks"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":[""],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD075810"],"sample_protocol":["Four datasets were analyzed for this work. These datasets supplement initial work; see PXD070310.<br><br>Dataset 1R: Synthetic peptide experiments (Af1521 incubation), related to Figure 1E and S1C-D, referred to as “DS1R”.<br>Dataset 2R: Synthetic peptide experiments (Af1521 pulldown), related to Figure 1E and S1E-F, referred to as “DS2R”.<br>Dataset 3R: Total proteome experiments, related to Figures S5, S6B-D, S7C-D, referred to as “DS3R”.<br>Dataset 4R: PARP1 in vitro auto-modification experiments, related to Figure S9, referred to as “DS4R”.<br><br>For DS1R and DS2R, peptides containing ADPr on specific moieties were generated essentially as described previously (Tashiro et al., 2022). For DS3R, total proteome analysis was performed on input samples corresponding to ADP-ribosylome purifications (see PXD070310). For DS4R, an in vitro PARP1 auto-modification reaction was performed, using recombinant PARP1 and PARP1 E988K. For full sample preparation details, please refer to “methods.docx”.<br><br>All samples (except total proteome; DS3R) were analyzed using an Orbitrap Fusion™ Lumos™ Tribrid™ mass spectrometer (Thermo), and analyzed on 15-cm long analytical columns with an internal diameter of 50 μm, packed in-house using ReproSil-Pur 120 C18-AQ 1.9 µm beads (Dr. Maisch). On-line reversed-phase liquid chromatography to separate peptides was performed using a Vanquish™ Neo UHPLC system (Thermo), and the analytical column was heated to 40°C using a column oven (Sonation). Peptides were eluted from the column using a gradient of Buffer A (0.1% formic acid) and Buffer B (80% ACN in 0.1% FA). For DS1R and DS2R, the primary gradient ranged from 5% B to 28% B over 11 minutes, followed by a washing block of 4 minutes. For DS4R, the primary gradient ranged from 5% B to 40% B over 14 minutes, followed by a washing block of 6 minutes. Electrospray ionization (ESI) was achieved using a Nanospray Flex NG Ion Source (Thermo). Spray voltage was set to 2 kV, capillary temperature to 275°C, and RF level to 40%. Full scans were performed at a resolution of 120,000, with a scan range of 300 to 1,300 m/z, a maximum injection time of 246 ms, and an automatic gain control (AGC) target of 600,000 charges. Precursors isolation was performed at a width of 1.3 m/z, an AGC target of 200,000 charges, and precursor fragmentation was accomplished using electron transfer disassociation with supplemental higher-collisional disassociation (EThcD) at 20 NCE, using calibrated charge-dependent ETD parameters (Rose et al., 2015). Precursors with charge state 2-6 (DS1R,2R) or 2-5 (DS4R) were isolated for MS/MS analysis, and for DS4R charge 3-5 were given (equal) top priority, followed by charge 2. Selected precursors were excluded from repeated sequencing by setting a dynamic exclusion of 0.6 s per minute (i.e. 1%) of total gradient time. MS/MS spectra were measured in the Orbitrap at a scan resolution of 60,000, and using a constant cycle time of 0.8 s (DS1R,2R) or 1.0 s (DS4R) with a maximum MS2 injection time of 250 ms.<br><br>For total proteome (DS3R), approximately 1 µg of peptide was analyzed per injection. Samples were analyzed on a Vanquish™ Neo UHPLC system (Thermo) coupled to an Orbitrap™ Astral™ mass spectrometer (Thermo). Samples were analyzed on 15-cm long analytical columns, with an internal diameter of 50 μm, and packed in-house using ReproSil-Pur 120 C18-AQ 1.9 µm beads (Dr. Maisch). The analytical column was heated to 40 °C, and elution of peptides from the column was achieved by application of gradients with stationary phase Buffer A (0.1% FA) and increasing amounts of mobile phase Buffer B (80% ACN in 0.1% FA). The primary analytical gradient ranged from 10 %B to 38 %B over 22.5 min, followed by a further increase to 48 %B over 2.5 min to elute any remaining peptides, and by a washing block of 3.75 min. Ionization was achieved using a NanoSpray Flex NG ion source (Thermo), with spray voltage set at 2 kV, ion transfer tube temperature to 275 °C, and RF lens to 50%. All full precursor (MS1) scans were acquired using the Orbitrap™ mass analyzer, while all tandem fragment (DIA) scans were acquired in parallel using the Astral™ mass analyzer. Full scan range was set to 300-1,000 m/z, MS1 resolution to 240,000, MS1 AGC target to “500” (5,000,000 charges), and MS1 maximum injection time to 30 ms. Precursors were analyzed in data-independent acquisition (DIA) mode, with isolation window width set to 4 m/z, maximum isolation time set to 5 ms, and DIA AGC target set to “200” (20,000 charges). Precursor mass range for DIA was set to 300-1000 m/z (175 windows) for the first technical replicate, and 302-998 m/z (174 windows) for the second technical replicate. Fragmentation was achieved using higher-energy collision disassociation (HCD) with normalized collision energy of 25, and fragment scan range was set to 150-1,500 m/z. Full scans were performed between each full set of DIA scans, resulting in a cycle time of ~0.9 s."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For DS1R and DS2R, analysis of the mass spectrometry raw data was performed using Skyline software (Pino et al., 2020). To this end, Skyline was provided with monoisotopic peptide information corresponding to each of the eight peptides, obtained via a pre-search of representative data files using MaxQuant software (Cox and Mann, 2008; Cox et al., 2011), version 1.5.3.30. C-terminal amidation was set as a fixed peptide modification. ADP-ribosylation was set as a variable modification, as well as tryptophan oxidation to kynurenin, as we observed this to be highly prevalent. Thus, Skyline was set up to identify and extract intensity profiles for the following 16 peptide sequences directly from the data. GWTARKSAEAGTAGK[−1], GW[+4]TARKSAEAGTAGK[−1], GWTAR[+541.1]KSAEAGTAGK[−1], GW[+4]TAR[+541.1]KSAEAGTAGK[−1], GWTARKSAAAGTAGK[−1], GW[+4]TARKSAAAGTAGK[−1], GWTARKS[+541.1]AAAGTAGK[−1], GW[+4]TARKS[+541.1]AAAGTAGK[−1], GWTARKAAEAGTAGK[−1], GW[+4]TARKAAEAGTAGK[−1], GWTARKAAE[+541.1]AGTAGK[−1], GW[+4]TARKAAE[+541.1]AGTAGK[−1], GWTARKAADAGTAGK[−1], GW[+4]TARKAADAGTAGK[−1], GWTARKAAD[+541.1]AGTAGK[−1], and GW[+4]TARKAAD[+541.1]AGTAGK[−1]. Extracted peptide intensities were normalized to total ion current, and variants of tryptophan oxidation were summed. To calculate the fraction of ADP-ribosylated peptide for each amino acid linkage, the intensity of their respective modified peptide was divided by the summed intensity of both unmodified and modified peptides.<br><br>For DS3R, analysis of the mass spectrometry raw data was performed using DIA-NN (Demichev et al., 2020), v1.9.2. For library-free search, the human FASTA database (105,529 entries) was downloaded from UniProt on the 13th of November, 2024, and DIA-NN was used to generate a spectral library in silico. To this end, settings used were Trypsin/P digestion (default), 2 missed cleavages, peptide length between 6 and 60, precursor charge state between 2 and 4, precursor m/z range from 300 to 1,000 m/z, and fragment ion m/z range from 100 to 1,500 m/z. RAW files were first converted to DIA format, after which they were searched with DIA-NN using the spectral library described above, with default settings. “MBR” was enabled, which generates a new spectral library based on a first search, which is then used to re-analyze the data. Global false discovery rate control was set to 1% (default). The “--matrix-spec-q” command was provided, to enforce a 1% FDR control at the run-specific level (in addition to the global FDR control).<br><br>For DS4R, analysis of the mass spectrometry raw data was performed using MaxQuant software (Cox and Mann, 2008; Cox et al., 2011), version 1.5.3.30. MaxQuant default settings were used, with exceptions outlined below. For generation of the theoretical spectral library, the PARP1 and PARP1-E988K sequences were used. N-terminal acetylation, methionine oxidation, cysteine carbamidomethylation, and ADP-ribosylation on all amino acid residues known to potentially be modified (C, D, E, H, K, R, S, T, and Y), were included as variable modifications. For the first search, which is only used for mass recalibration, no variable modifications were used. Up to 8 missed cleavages were allowed, a maximum allowance of 3 variable modifications per peptide was used, and maximum peptide mass was set to 6,000 Da. First and main search precursor mass tolerances of 10 and 4.5 ppm were used, respectively. For fragment ion masses, a tolerance of 20 ppm was used. Data was automatically filtered by posterior error probability to achieve a false discovery rate of <1% (default), at the peptide-spectrum match and the protein assignment levels."],"omics_type":["Proteomics"],"labhead":["Sara Buch-Larsen"],"instrument_platform":[""],"labhead_affiliation":["Proteomics program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["ivo.a.hendriks@gmail.com"],"publication":["10.1038/S41467-026-73677-X"],"submitter_affiliation":["Proteomics program, Novo Nordisk Foundation Center for Protein Research, Faculty of Health and Medical Sciences, University of Copenhagen, Blegdamsvej 3B, 2200 Copenhagen, Denmark"],"submitter_country":["Denmark"],"additional_accession":[]},"is_claimable":false,"name":"Deciphering cytokine-driven ADP-ribosylation signaling networks via Af1521-based mass spectrometry analysis of labile Glu/Asp-linkages (REVISION)","description":"ADP-ribosylation (ADPr) is a regulatory post-translational modification targeting nine amino acid residues, but glutamate/aspartate-linked ADPr (Glu/Asp-ADPr) is labile and remains challenging to detect using conventional mass spectrometry (MS)-based workflows. Using synthetic peptides, we show that ester-linked Glu/Asp-ADPr is lost under alkaline conditions, elevated temperatures, and by hydrolysis via wildtype Af1521. We developed an acidic enrichment workflow incorporating an Af1521 mutant that preserves Glu/Asp-ADPr, enabling site-specific, system-wide MS analysis. In cytokine-stimulated A549 and HeLa cells, we identified >600 Glu/Asp- and >200 Cys-ADPr sites. Glu/Asp-ADPr marks cytoplasmic, immune-related protein networks, contrasting with nuclear Ser-ADPr. Quantitative profiling revealed reproducible, cell type- and treatment-specific patterns. PARP10-mediated Glu/Asp ADPr of ubiquitin indicates direct crosstalk with ubiquitin signaling pathways. Interferon treatments revealed conserved antiviral PARP networks extensively modified on Glu/Asp residues. Together, our work establishes a robust MS-based workflow and provides a resource of site-specific ADPr events, revealing residue-specific ADPr in innate immune signaling.","dates":{"publication":"2026-05-27","submission":"2026-03-18"},"accession":"PXD075810","cross_references":{"TAXONOMY":["NEWT:6945","NEWT:184922","NEWT:6703","NEWT:3555","NEWT:2","NEWT:157546","NEWT:35554","NEWT:38942","NEWT:307972","NEWT:32046","NEWT:544496","NEWT:2102","NEWT:2042546","NEWT:259447","NEWT:45351","NEWT:43179","NEWT:4513","NEWT:5722","NEWT:1247","NEWT:1129","NEWT:376741","NEWT:55153","NCBITaxon:10407","NEWT:1736309","NEWT:309800","NEWT:281395","NEWT:10360","NEWT:1211601","NEWT:876138","NEWT:47664","NEWT:317548","NEWT:3654","NEWT:237561","NEWT:5833","NEWT:6928","NEWT:10036","NEWT:36745","NEWT:498019","NEWT:1351","NEWT:1438992","NEWT:1352","NEWT:2649997","NEWT:272563","NEWT:224326","NCBITaxon:79857","NEWT:1096976","NEWT:82688","NEWT:95648","NEWT:3885","NEWT:3888","NEWT:5821","NEWT:1589","NEWT:135622","NCBITaxon:4896","NEWT:6915","NEWT:3649","NEWT:101510","NEWT:28903","NEWT:3880","NEWT:272559","NEWT:28909","NEWT:515849","NEWT:3641","NEWT:383379","NEWT:466585","NEWT:10029","NEWT:913645","NEWT:1000589","NEWT:85963","NEWT:85962","NEWT:143361","NEWT:317447","NEWT:7955","NEWT:7959","NEWT:2261","NEWT:31156","NEWT:398580","NEWT:4442","NEWT:4565","NEWT:1264690","NEWT:515619","NEWT:192875","NEWT:34305","NEWT:59729","NCBITaxon:183674","NEWT:224308","NEWT:84645","NEWT:44586","NEWT:626528","NEWT:3347","NEWT:139927","NEWT:4558","NEWT:209285","NEWT:5888","NEWT:211586","NEWT:747078","NEWT:1282","NEWT:1283","NEWT:931281","NEWT:4550","NEWT:1000561","NEWT:294381","NEWT:197","NEWT:1390363","NEWT:77133","NEWT:288705","NEWT:29176","NCBITaxon:79824","NEWT:4787","NCBITaxon:4563","NEWT:5755","NEWT:44689","NEWT:3218","NEWT:5759","NEWT:1736231","NEWT:556182","NEWT:1270","NEWT:374990","NEWT:1392","NEWT:498217","NEWT:156471","NEWT:2242","NEWT:4784","NEWT:11320","NEWT:360106","NEWT:156476","NEWT:286","NEWT:391619","NEWT:360104","NEWT:287","NEWT:246197","NEWT:10117","NEWT:10239","NEWT:10116","NEWT:1280","NEWT:1735272","NEWT:83334","NEWT:83332","NEWT:44685","NEWT:317513","NEWT:1148","NEWT:580240","NEWT:5508","NEWT:294128","NEWT:11676","NEWT:55571","NEWT:35500","NEWT:1140","NEWT:100226","NEWT:4530","NEWT:1143","NEWT:4896","NEWT:75058","NEWT:13616","NEWT:1390","NEWT:1094343","NEWT:1336795","NEWT:172","NEWT:296543","NEWT:316435","NEWT:1773","NEWT:1895","NEWT:1182590","NEWT:3712","NEWT:82380","NEWT:105023","NEWT:866628","NEWT:935293","NEWT:64152","NEWT:4924","NEWT:749200","NEWT:375146","NEWT:990346","NEWT:145953","NEWT:257309","NEWT:100816","NEWT:263","NEWT:230741","NEWT:52283","NEWT:284812","NEWT:8175","NCBITaxon:1313","NEWT:43330","NEWT:1603293","NEWT:408169","NEWT:44544","NEWT:47946","NEWT:4911","NEWT:645463","NEWT:3702","NEWT:129249","NEWT:243277","NEWT:990119","NEWT:2850","NEWT:408172","NEWT:227321","NEWT:408170","NEWT:493760","NEWT:106590","NEWT:260710","NEWT:257313","NEWT:3827","NEWT:400772","NEWT:3708","NEWT:128161","NEWT:332648","NEWT:106592","NEWT:536231","NEWT:46704","NEWT:1436733","NEWT:460519","NEWT:1187947","NEWT:1432138","NEWT:269796","NEWT:10312","NEWT:1424507","NCBITaxon:1773","NEWT:54571","NEWT:9598","NEWT:8030","NEWT:9483","NCBITaxon:40559","NEWT:1639","NEWT:188229","NEWT:3818","NEWT:480","NEWT:4909","NEWT:67767","NEWT:759272","NEWT:432359","NEWT:46835","NEWT:1182263","NEWT:109757","NEWT:943146","NEWT:2711","NEWT:300852","NEWT:1502","NEWT:376686","NEWT:95486","NEWT:9103","NEWT:1883446","NEWT:29159","NEWT:253","NEWT:10306","NCBITaxon:2759","NEWT:1233435","NEWT:93061","NEWT:8022","NEWT:145943","NCBITaxon:4932","NEWT:595536","NEWT:240906","NEWT:593117","NEWT:89920","NEWT:3635","NEWT:5811","NEWT:235443","NEWT:180923","NEWT:108458","NEWT:272623","NEWT:272624","NEWT:411483","NEWT:884019","NEWT:198215","NEWT:411490","NEWT:983964","NEWT:118499","NEWT:169963","NEWT:32644","NEWT:527796","NEWT:225117","NEWT:746128","NEWT:499175","NEWT:109779","NEWT:43665","NEWT:1266464","NEWT:476272","NEWT:3747","NEWT:195051","NEWT:367830","NEWT:1255228","NEWT:178616","NEWT:649908","NEWT:410289","NEWT:373153","NEWT:375451","NEWT:352472","NEWT:357","NEWT:1071661","NEWT:360094","NEWT:470","NEWT:41364","NEWT:1313","NEWT:411469","NEWT:84023","NEWT:559292","NEWT:39491","NCBITaxon:5811","NEWT:29491","NEWT:411464","NEWT:411460","NEWT:2014887","NEWT:2762","NEWT:1174673","NEWT:1328426","NEWT:562","NEWT:411470","NEWT:33952","NEWT:2094720","NCBITaxon:2697049","NEWT:571256","NEWT:40483","NEWT:28038","NEWT:1663","NEWT:1423","NEWT:4932","NEWT:3603","NEWT:2759","NEWT:3847","NEWT:38293","NEWT:1428","NEWT:327159","NEWT:178876","NEWT:1660","NEWT:327160","NEWT:573","NEWT:9031","NEWT:1872122","NEWT:7091","NEWT:108931","NEWT:241368","NEWT:1055524","NEWT:42528","NEWT:190802","NEWT:9778","NEWT:150475","NEWT:303","NEWT:9417","NEWT:7111","NEWT:347515","NEWT:1216979","NEWT:7237","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:115104","NEWT:1121114","NEWT:663","NEWT:1081927","NEWT:1238993","NEWT:67825","NEWT:187878","NEWT:185579","NEWT:941442","NEWT:220668","NEWT:13076","NEWT:1821314","NEWT:1249668","NEWT:7108","NEWT:317","NEWT:5286","NEWT:7227",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