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Dziembowski"],"software":["Not available"],"tissue":["Erythrocyte","Liver"],"sample_protocol":["TurboID-nanobody construct was introduced to cells by lentiviral transduction. Virus production and transduction methods were described in separate sections. After 48h of culture, cells from 6 wells of 12-well plate were pooled (approximately 4 × 107 cells) following washing with PBS and resuspension in 6ml erythroblasts differentiation medium (described in separate section) containing 500 µM biotin (B4501, Sigma-Aldrich) following 15 min incubation at 37°C. Cells were collected on ice to stop the biotinylation and all following steps including the lysate handling and pulldown were done in 4°C to avoid biotinylation in vitro. Cells were washed with ice cold PBS and spun 800 × g/ 4°C for 5 min. Washing was repeated 2 times. To evaluate the robustness of the assay we fixed 5 × 105 of acquired cells and stained them with Streptavidin fluorescent conjugate as described in flow cytometry section. The remaining cells were lysed in 1 ml RIPA buffer with protease inhibitors and protein concentration was quantified as described in the protein extraction section. All washes performed downstream were carried out by resuspension of the beads in specific buffer, 2min rotation and magnetic separation followed by rejection of the supernatant. For pull-down of biotinylated proteins we used Pierce Streptavidin Magnetic Beads (88817, Thermo Scientific) which were equilibrated by washing twice in RIPA buffer prior to incubation with the lysate. We used 1mg of equilibrated beads per 0,5 mg of protein with lysate final concentration kept at 1 mg/ml protein. Beads were incubated with the lysate overnight in 4°C. Beads were separated and supernatant was retained as flow-through fraction. Beads were subjected to a series of washes: 2x with RIPA devoid of Triton X-100, 1x in KCL, 1x in 100 mM Na2CO3, 1x in 2M urea, 2x with RIPA devoid of Triton X-100 and 2x in 50mM Tris-HCl pH = 7,5. After last wash beads were separated, supernatant was discarded following short centrifugation 10s / 10000 × g /4 °C and residual liquid was removed while the tube was on the magnetic stand. Dry beads were kept in –80°C until further processed. For each sample, 100 µL of 100 mM ammonium bicarbonate and 2.5 µL of 200 mM tris(2-carboxyethyl)phosphine (TCEP) were added. Samples were vortexed briefly and placed on a horizontal shaker set to 10,000 rpm at room temperature for 30 min. Next, 2 µL of methyl methanethiosulphonate (MMTS) were added, and the samples were shaken for an additional 20 min at room temperature. Trypsin/LysC mix, prepared in 8 M urea with 100 mM ammonium bicarbonate to a final enzyme concentration of 0.02 µg/µL, was added to the samples (50 µL per sample). The samples were incubated at 37°C for 4 h with shaking, after which 300 µL of 100 mM ammonium bicarbonate was added. Digestion was allowed to proceed overnight. Following digestion, the samples were acidified with 10 µL of 5% trifluoroacetic acid (TFA). Tryptic peptides were purified using a modified SP3 protocol71 and subsequently vacuum-dried. Samples were analyzed on an EvosepOne (Evosep Biosystems) online LC-MS system coupled to an Orbitrap Exploris 480 mass spectrometer (Thermo Fisher Scientific). Peptide mixtures were loaded onto C18 Evotip trap columns, following the manufacturer’s protocol. This involved activation of the sorbent with 0.1% formic acid (FA) in acetonitrile, a 2-minute incubation in 1-propanol, and equilibration of the chromatographic sorbent with 0.1% FA in water. Samples were loaded in 30 µL of 0.1% FA, with centrifugation at 600 × g for 1 minute after each step."],"repository":["Pride"],"labhead":["Andrzej Dziembowski"],"instrument_platform":[""],"labhead_affiliation":["Laboratory of RNA Biology, International Institute of Molecular and Cellular Biology"],"submission_type":["COMPLETE"],"publication":["Not available"],"submitter_affiliation":["International Institute of Molecular and Cell Biology in Warsaw, Poland"],"labhead_mail":["adziembowski@iimcb.gov.pl"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"disease":["Disease Free"],"submitter_keywords":["Erythropoiesis","Interactome","Cytoplasmic polyadenylation","Tent5c"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD072661"],"quantification_method":[""],"modification":[""],"data_protocol":["Chromatographic separation was performed at a flow rate of 500 nL/min using the 44-minute (30 samples per day) gradient on an EV1106 analytical column (Dr. Maisch C18 AQ, 1.9 µm beads, 150 µm ID, 15 cm long, Evosep Biosystems, Odense, Denmark). Data acquisition was carried out in positive ion mode using a data-dependent acquisition (DDA) method. MS1 scans were acquired at a resolution of 60,000 with a normalized AGC target of 300%, auto maximum injection time, and a scan range of 350–1400 m/z. MS2 scans were performed at a resolution of 15,000, using a top-40 method with a precursor isolation window of 1.6 m/z. Dynamic exclusion was set to 20 s with a mass tolerance of ±10 ppm, and the precursor intensity threshold was set to 5 × 1000. Fragmentation was achieved using higher-energy collisional dissociation (HCD) at a normalized collision energy of 30%. The spray voltage was set to 2.1 kV, with a funnel RF level of 40 and a heated capillary temperature of 275°C."],"omics_type":["Proteomics"],"species":["Mus Musculus (mouse)"],"submitter_mail":["adziembowski@iimcb.gov.pl"],"submitter_country":["Poland"],"doi":["10.6019/PXD072661"],"additional_accession":[]},"is_claimable":false,"name":"Efficient globin production during terminal erythropoiesis depends on the cooperative action of TENT5C poly(A) polymerase and LARP4B in mice","description":"To identify erythroid-specific TENT5C interactors, we employed a modified TurboID proximity biotinylation assay followed by MS/MS analysis of fetal liver erythroblasts differentiated ex vivo. We took advantage of Tent5c-EGFP knock-in mouse line and employed lentiviral vector expressing nanobody anti-EGFP fused with TurboID biotinylase. By introducing this construct to either WT or Tent5c-EGFP erythroblasts, we were able to quantitatively determine the specificity of enriched proteins found in proximity to TENT5C-EGFP compared to the background found in the WT. This approach does not require the introduction of exogenous biotinylase-tagged TENT5C, which expression would be out of place in the earliest stages of erythropoiesis. Importantly, it was designed for the knock-in model in which the expression timing for TENT5C is in accord with the developmental timeline of erythroblasts. Hence, we expected the enriched proximal proteins to be physiologically relevant interactors of TENT5C.","dates":{"publication":"2026-06-29","submission":"2026-01-05"},"accession":"PXD072661","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:592321","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:294671","NEWT:376619","NEWT:1748418","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:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:166340","NEWT:10029","NEWT:913645","NEWT:2492962","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:111225","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:55350","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:1912919","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","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:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","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:1538","NEWT:2065263","NEWT:199225","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:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","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:31345","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:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","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:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","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:299467","NEWT:9541","NEWT:51350","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","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