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The following liquid chromatography buffers were used: buffer A (0.1% formic acid in Milli-Q water (v/v)) and buffer B (80% acetonitrile and 0.1% formic acid in Milli-Q water (v/v). Samples were loaded at 10 μl/min onto a trap column (100 μm × 2 cm, PepMap nanoViper C18 column, 5 μm, 100 Å, Thermo Scientific) equilibrated in 0.1% trifluoroacetic acid (TFA). The trap column was washed for 3 min at the same flow rate with 0.1% TFA then switched in-line with a Thermo Scientific, resolving C18 column (75 μm × 50 cm, PepMap RSLC C18 column, 2 μm, 100 Å). Peptides were eluted from the column at a constant flow rate of 300 nl/min with a linear gradient from 3% buffer B to 6% buffer B in 5 min, then from 6% buffer B to 35% buffer B in 115 min, and finally to 80% buffer B within 7 min. The column was then washed with 80% buffer B for 4 min and re-equilibrated in 3% buffer B for 15 min. Two blanks were run between each sample to reduce carry-over. The column was kept at a constant temperature of 50 °C.   The data was acquired using an easy spray source operated in positive mode with spray voltage at 2.445 kV, and the ion transfer tube temperature at 250 °C. The MS was operated in DIA mode. A scan cycle comprised a full MS scan (m/z range from 350 to 1650), with RF lens at 40%, AGC target set to custom, normalised AGC target at 300%, maximum injection time mode set to custom, maximum injection time at 20 ms, microscan set to 1 and source fragmentation disabled. MS survey scan was followed by MS/MS DIA scan events using the following parameters: multiplex ions set to false, collision energy mode set to stepped, collision energy type set to normalized, HCD collision energies set to 25.5, 27 and 30%, orbitrap resolution 30,000, first mass 200, RF lens 40%, AGC target set to custom, normalized AGC target 3000%, microscan set to 1 and maximum injection time 55 ms. Data for both MS scan and MS/MS DIA scan events were acquired in profile mode."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Data independent (DIA) mass spectrometry raw files were searched using Spectronaut (Biognosys) version 19. Raw mass spec files were searched against a mouse data base (Swissprot Trembl November 2023) with the following parameters: directDIA, false discovery rate set to 1%, protein N-terminal acetylation and methionine oxidation were set as variable modifications and carbamidomethylation of cysteine residues was selected as a fixed modification. Copy numbers were calculated using the proteomic ruler (Wisniewski et al., 2014) using Perseus software."],"omics_type":["Proteomics"],"labhead":["Dr Andy Howden"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["School of Life Sciences, University of Dundee, Dow Street, Dundee, DD1 5EH, UK"],"species":["Mus Musculus (mouse)"],"publication":["Not available"],"submitter_mail":["a.howden@dundee.ac.uk"],"submitter_affiliation":["University of Dundee"],"submitter_country":["United Kingdom"],"additional_accession":[]},"is_claimable":false,"name":"A proteomic map of B cell activation and its shaping by mTORC1, MYC and iron - synergy data","description":"Using high resolution quantitative mass spectrometry, we have explored how immune activation and the metabolic checkpoint kinase mTORC1 (mammalian target of rapamycin complex 1) regulate the proteome of B lymphocytes. B cell activation via the B cell receptor, CD40 and the IL-4 receptor induced considerable re-modelling of the B cell protein landscape, with a 5-fold increase in total cellular protein mass within 24 hours of activation. Analysis of copy numbers per cell of >7,500 proteins revealed increases in the metabolic machinery that supports B cell activation and nutrient and amino acid transporters that fuel B cell biosynthetic capacity. Comparison of T cell-dependent versus T cell-independent B cell stimulation along with an analysis of the synergistic effects of stimuli, identified shared and unique impacts of stimuli and highlighted the drivers of B cell proteome remodelling. In addition, we reveal that mTORC1 controls activation-induced B cell growth and inhibiting mTORC1 impairs the expression of amino acid transporters that fuel B cell protein production. We also show that mTORC1 activity regulates the expression of the transcription factor MYC and the transferrin receptor CD71. Blocking MYC activity phenocopied mTORC1 inhibition in many ways including impaired CD71 expression, while limiting iron availability during B cell activation impaired B cell growth and protein synthesis. This work provides a detailed map of naïve and immune activated B cell proteomes and a greater understanding of the cellular machinery that direct B cell phenotypes. This work also provides new insights into the role of mTORC1, MYC and iron in regulating activation-induced proteome remodelling and protein production in B 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