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 Singh"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Rsk1","Ifng","Humanized mice","Pbmc","Macrophage"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD069750"],"tissue":["Primary Cell","Cell Culture"],"sample_protocol":["Subcellular fractionation We used ProteoExtract Subcellular Proteome Extraction Kit (EMD Millipore) to obtain nuclear lysates of human macrophages in according to the instructions of the manufacturer.  Tandem mass tagging (TMT) sample preparation  We stimulated human PBMC-derived macrophages obtained from three donors (donor A, #44383; donor B, #44442; donor C, #44400) with IFN-γ for 0, 10, 20, 30, or 60 minutes. Nuclear fractions of each condition were isolated using ProteoExtract Subcellular Proteome Extraction Kit (EMD Millipore) and proteolysed (Lys-C, Wako Chemicals) using in-solution urea strategy detailed previously (35). Peptides were labeled with TMT 10-plex reagent (Pierce). The reporter ion channels were assigned for two sets of running as follows: for first running, 126 (0 minutes with IFN-γ, donor A), 127N (10 minutes with IFN-γ, donor A), 128N (20 minutes with IFN-γ, donor A), 129N (30 minutes with IFN-γ, donor A), 130N (60 minutes with IFN-γ, donor A), 127C (60 minutes with IFN-γ, donor B), 128C (30 minutes with IFN-γ, donor B), 129C (20 minutes with IFN-γ, donor B), 130C (10 minutes with IFN-γ, donor B) and 131 (0 minutes with IFN-γ, donor B); for second running, 126 (0 minutes with IFN-γ, donor A), 127N (10 minutes with IFN-γ, donor A), 128N (20 minutes with IFN-γ, donor A), 129N (30 minutes with IFN-γ, donor A), 130N (60 minutes with IFN-γ, donor A), 127C (60 minutes with IFN-γ, donor C), 128C (30 minutes with IFN-γ, donor C), 129C (20 minutes with IFN-γ, donor C), 130C (10 minutes with IFN-γ, donor C) and 131 (0 minutes with IFN-γ, donor C). The labeled peptides were combined and desalted using Oasis Hlb 1 cc columns (Waters). The peptides were then fractionated into 24 fractions based on their isoelectric focusing point (pH range of 3-10) using the OFF-gel system (Agilent). The fractions were dried using a tabletop speed vacuum, cleaned with the Oasis columns and resuspended in 40 µl of 5% acetonitrile and 0.5% formic acid for subsequent analysis by liquid chromatography/mass spectrometry (LC/MS)."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["Liquid chromatography tandem mass spectrometry (LC-MS/MS) TMT studies - The high resolution/accuracy Q Exactive mass spectrometer fronted with a Nanospray FLEX ion source, coupled to an Easy-nLC1000 HPLC pump (Thermo Scientific) was used to analyze the TMT peptide samples. The analytical gradient was run at 300 nl/minutes from 5 to 18% Solvent B (acetonitrile/0.1 % formic acid) for 120 minutes, followed by five minutes of 95% Solvent B. Solvent A was 0.1 % formic acid. The precursor scan was set to 140 K resolution, and the top 10 precursor ions (within a scan range of 380-2000 m/z) were subjected to higher energy collision induced dissociation (HCD, collision energy 30%, isolation width 3.0 m/z, dynamic exclusion enabled, starting m/z fixed at 120 m/z, and resolution set to 35 K) for peptide sequencing (MS/MS).  Anti-STAT1-pSer727 IPs - The STAT1 peptide with phosphorylation at Ser727 was detected on the Orbitrap Fusion Lumos. The gradient flow rate was 300 nL/min from 5 to 21 % solvent B (acetonitrile/0.1 % formic acid) for 80 minutes, 21 to 30% solvent B for ten minutes, followed by five minutes of 95% solvent B. Solvent A was 0.1% formic acid. The target phosphorylated STAT1 peptide, LQTTDNLLPmsPEEFDEVSR (m10-oxidation, s11-phosphorylation, 806.3575 m/z, z=3), was subjected to EThcD (calibrated charge dependent ETD parameters enabled, HCD collision energy 30%, and resolution set to 500 k) for MS/MS.   LC-MS/MS data analysis TMT studies - The MS/MS data were queried against the human UniProt database (downloaded on August 1, 2014) using the SEQUEST search algorithm, via the Proteome Discoverer version 2.1 (PD2.1, Thermo Fisher Scientific), using a 10-ppm tolerance window in the MS1 search space, and a 0.02 Da fragment tolerance window for HCD. Methionine oxidation was set as a variable modification, and carbamidomethylation of cysteine residues and 10-plex TMT tags (Thermo Fisher Scientific) were set as fixed modifications. The peptide false discovery rate (FDR) was calculated using Percolator provided by PD: the FDR was determined based on the number of MS/MS spectral hits when searched against the reverse, decoy human database. Peptides were filtered based on a 1% FDR. Peptides assigned to a given protein group, and not present in any other protein group, were considered as unique. Consequently, each protein group is represented by a single master protein (PD Grouping feature). Master proteins with two or more unique peptides were used for TMT reporter ratio quantification. The normalized reporter ion intensities were exported from PD2.1 the analysis below."],"omics_type":["Proteomics"],"labhead":["Masanori Aikawa"],"instrument_platform":[""],"labhead_affiliation":["Center for Interdisciplinary Cardiovascular Sciences, Cardiovascular Division, Department of Medicine, Brigham and Women’s Hospital, Harvard Medical School, Boston, Massachusetts 02115, U.S.A."],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"submitter_mail":["sasingh@bwh.harvard.edu"],"publication":["10.1126/SCIADV.ADY4193"],"submitter_affiliation":["Brigham and Women's Hospital, Harvard Medical School"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Nuclear RSK1 mediates interferon γ-induced pro-inflammatory activation in human primary macrophages and humanized mice","description":"Pro-inflammatory activation of macrophages promotes various inflammatory disorders. The molecular mechanisms underlying macrophage activation, particularly in the context of nuclear translocation of pro-inflammatory response mediators, remain obscure. We have used a systems approach to explore key regulators of macrophage activation using quantitative proteomics to monitor protein translocation to the nuclei of human primary macrophages elicited with interferon γ (IFN-γ). Unbiased bioinformatics identified several candidates, including RSK1, a ribosomal protein kinase. Network analysis linked RSK1 with human gene modules for various inflammatory disorders. In vitro mechanistic experiments showed that IFN-γ stimulation promotes RSK1 phosphorylation at Ser380 via JAK signaling, resulting in STAT1 phosphorylation at Ser727, in the nuclei of macrophages. In concert with these results, RSK1 silencing or deficiency hinders IFN-γ-induced secretion of pro-inflammatory chemokines in human primary macrophages. Furthermore, RSK1 deficiency in human leukocytes altered IFN-γ-induced responses in humanized mice. Our findings provide evidence that RSK1 is a key nuclear shuttling enzyme that mediates pro-inflammatory activation of macrophages.","dates":{"publication":"2026-07-08","submission":"2025-10-22"},"accession":"PXD069750","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:475174","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:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","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:156587","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:28174","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:8165","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:55784","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:1185650","NEWT:216778","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","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:1255228","NEWT:410289","NEWT:373153","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:470","NEWT:5911","NEWT:748693","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:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","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:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","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:99488","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:441772","NEWT:48106","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:300273","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:4236","NEWT: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