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Liu"],"technology_type":["Mass Spectrometry","Bottom-up proteomics"],"disease":["Kidney Cancer"],"software":[""],"submitter_keywords":["Phosphorylation","Egf","Tunicamycin","Proteomic","Glycosylation"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD071440"],"tissue":["Cell Culture","Kidney Cell"],"sample_protocol":["Cell culture and treatments A498 cells (ATCC HTB-44) were cultured at 37 °C with 5% CO₂ in MEM (Gibco 11095080) containing 10% FBS and 1% Pen/Strep. For tunicamycin treatment, cells were exposed to 0.005, 0.01, 0.05, 0.1, 0.5, 1, 5, and 10 μM tunicamycin (Selleck S7894), plus a DMSO control, for 24 h. Afterward, cells were treated with or without 50 ng/ml EGF (Sigma E9644) for 15 min. Cells were washed with cold PBS and harvested, yielding approximately 4 million cells per condition.  Protein extraction and digestion Cell pellets were lysed on ice using 100 μl of buffer containing 8 M urea, 75 mM NaCl, 50 mM Tris pH 8.0, 1 mM EDTA, protease inhibitors (2 μg/ml aprotinin, 10 μg/ml leupeptin, 1 mM PMSF), phosphatase inhibitors (10 mM NaF, PIC2 and PIC3 at 1:100), and 20 μM PUGNAc. Lysis included vortexing and repeated incubation cycles at 4 °C. Lysates were cleared by centrifugation (20,000 g, 10 min) and protein levels were measured by BCA assay. Proteins were adjusted to 5 μg/μl, and 500 μg aliquots were prepared.  Proteins were reduced with 6 mM DTT (1 h, 37 °C) and alkylated with 12 mM IAA (45 min, dark). Samples were diluted 1:4 with 50 mM Tris pH 8.0 to reduce urea below 2 M. Proteins were digested with LysC (1:50, 2 h, 25 °C), followed by trypsin (1:50, ~14 h, 25 °C). Digestion was stopped by adding formic acid to 1% final concentration (pH 3). Samples were diluted to 1 ml with 0.1% FA, centrifuged to remove precipitates, desalted by C18 SPE, and dried.  TMT labeling For each TMT18 channel, 250 μg peptides (measured by peptide BCA) were dissolved in 100 μl 100 mM HEPES pH 8.5. TMT reagent was reconstituted in anhydrous ACN, and 500 μg reagent was added per sample (1:2 peptide:TMT). Labeling occurred for 1.5 h at room temperature with shaking. Reactions were quenched with 5% hydroxylamine (15 min). Labeled samples were pooled, dried, reconstituted in 3% ACN/0.1% FA, pH-adjusted to 3 if needed, and cleaned again on SepPak cartridges.  Peptide fractionation Dried peptides were resuspended in 20 mM ammonium formate (pH 10) with 2% ACN and separated by basic reversed-phase HPLC (Agilent 1200) on a Zorbax Extend-C18 column. Peptides were eluted using a multi-step gradient of Solvent A (2% ACN, 5 mM ammonium formate) and Solvent B (90% ACN, 5 mM ammonium formate). Fractions were collected and concatenated into 24 pools. Five percent of each fraction was dried and resuspended in 3% ACN/0.1% FA for global proteomics; the remaining material was used for phosphopeptide enrichment.  Phosphopeptide enrichment (Fe-IMAC) Concatenated peptides were resuspended in 80% ACN/0.1% TFA and incubated with Fe³⁺-NTA IMAC beads for 30 min. After removing unbound peptides, beads were washed and transferred to C18 StageTips. Phosphopeptides were eluted with 500 mM potassium phosphate (pH 7.0), cleaned on C18 StageTips, dried, and reconstituted in 3% ACN/0.1% FA for LC-MS/MS.  Glycopeptide enrichment (ZIC-HILIC) ZIC-HILIC micro-columns were prepared in-house and equilibrated with 80% ACN/1% TFA. Peptides were loaded, washed with the same buffer, and glycopeptides were eluted using 0.1% TFA. Eluates were dried and stored at –80 °C before LC-MS/MS analysis."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["LC-MS/MS analysis All LC-MS/MS data were acquired using an EvoSep system coupled to an Orbitrap Fusion Ascend mass spectrometer (Thermo Scientific) operating in data-dependent acquisition (DDA) mode. TMT-labeled global proteome, phosphoproteome, and glycoproteome fractions were loaded onto Evotips and separated on a PepSep C18 column (15 cm × 150 µm, 1.5 µm) at 50 °C using a 30 SPD gradient.  For global and phosphoproteomic samples, MS1 scans were collected at 60,000 resolution across 350–1800 m/z with an AGC target of 4×10⁵, max injection time of 50 ms, RF lens of 30%, and charge states 2–6. Dynamic exclusion was set at 45 s. A 2-s cycle time was used, selecting the most abundant precursors for MS2. MS2 spectra were acquired at 50,000 resolution using HCD at 34% collision energy, 0.7 m/z isolation width, AGC 2×10⁵, and max injection time of 100 ms.  For glycoproteomic samples, MS1 scans were acquired at 60,000 resolution from 500–2000 m/z with AGC 5×10⁵. MS2 scans used 50,000 resolution, HCD 35%, 0.7 m/z isolation width, AGC 1×10⁵, and 100 ms injection time. Source settings were 1.8 kV spray voltage and 300 °C ion transfer tube temperature. Additional glycoproteomic runs employed stepped HCD energies (25/35/45%), MS1 at 120,000 resolution, and MS2 at 30,000 resolution (AGC 3×10⁵, 64 ms injection time). Charge states 2–8 and a dynamic exclusion of 45 s (±10 ppm) were applied.  MaxQuant analysis for global, phospho-, and glycoproteomic data Raw files were processed with MaxQuant (v2.4.14.0) using the UniProtKB human reference proteome (downloaded 2024-02-29). Trypsin specificity was used with up to 3 missed cleavages for global samples and 4 for PTM datasets. Fixed modification: carbamidomethyl-Cys; variable modifications: Met oxidation and N-terminal acetylation. Phospho-Ser/Thr/Tyr was allowed for phosphoproteomic datasets. Peptides required ≥6 amino acids, with up to 5 modifications per peptide. Modified peptides required an Andromeda score ≥40 and delta score ≥6.  A 1% PSM FDR was applied using a target–decoy strategy. For PTM datasets, the protein-level FDR was set to 100% to maintain a 1% FDR at the peptide level; protein groups were not used for PTM quantification. For global proteomics, the protein FDR was set at 1%. TMT isotope impurities were corrected automatically. The phosphoproteome evidence file and global proteome proteinGroups file were used for quantification.  Glycoproteomic data processing (GPQuest)  DDA glycoproteomic raw files were converted to mzML using ProteoWizard (peak picking enabled). Glycopeptide identification was performed using GPQuest 3.0 with a human N-glycan library and the same UniProtKB database.  Search parameters included: precursor tolerance 10 ppm, fragment tolerance 20 ppm, trypsin digestion with up to 2 missed cleavages, peptide length 7–50 aa, and precursor charge states +2 to +8. b- and y-ions were considered for peptide fragmentation, requiring at least 6 matched peaks. Carbamidomethyl-Cys was set as fixed and Met oxidation as variable. Identifications were filtered at 1% PSM FDR."],"omics_type":["Proteomics"],"labhead":["Hongyi Liu"],"instrument_platform":[""],"labhead_affiliation":["Johns Hopkins University"],"submission_type":["PARTIAL"],"species":["Homo Sapiens (human)"],"publication":["41843583 Liu H, Lin DC, Hu Y, Sun Z, Huang Y, Xu Y, Zhang H. Dose-Dependent Inhibition of Protein Glycosylation Reveals Crosstalk between Glycosylation and Phosphorylation in EGF Signaling Pathways. Anal Chem. 2026 98(12):9293-9304 10.1021/acs.analchem.5c08113"],"submitter_mail":["hliu173@jh.edu"],"submitter_affiliation":["Johns Hopkins University"],"submitter_country":["United States"],"pubmed_abstract":["Protein glycosylation and phosphorylation play critical roles in regulating diverse cellular processes, yet their interplay remains underexplored. This study employed dose-dependent glycosylation inhibition to investigate the function of glycosylation, especially in phosphorylation in epidermal growth factor (EGF) signaling. Using quantitative proteomics, we analyzed global protein expression, glycopeptides, and phosphopeptides in EGF-stimulated and unstimulated conditions. Results revealed that glycosylation inhibition disrupted phosphorylation patterns in EGF-regulated pathways. Notably, 215 EGF-regulated phosphopeptides exhibited dose-dependent changes, with pathways such as ERBB, MAPK, and mTOR signaling being significantly affected. Protein-protein interaction analysis highlighted glycosylation-dependent modulation of phosphorylation in cytoskeletal remodeling and growth factor signaling. Correlation analysis identified site-specific glycopeptides, such as Asn568 of EGFR, that influenced phosphorylation of downstream signaling proteins. Additionally, individual proteins like RCN1 and SLC4A7 demonstrated glycosylation- and phosphorylation-regulated patterns. These findings underscored the role of glycosylation in maintaining phosphorylation-dependent signaling fidelity, providing insights into the function of glycosylation on cell signaling pathways."],"pubmed_title":["Dose-Dependent Inhibition of Protein Glycosylation Reveals Crosstalk between Glycosylation and Phosphorylation in EGF Signaling Pathways."],"pubmed_authors":["Liu Hongyi H, Lin Ding Chiao DC, Hu Yingwei Y, Sun Zhenyu Z, Huang Yuanyu Y, Xu Yuanwei Y, Zhang Hui H"],"additional_accession":[]},"is_claimable":false,"name":"Dose-Dependent Inhibition of Protein Glycosylation Reveals Crosstalk Between Glycosylation and Phosphorylation in EGF Signaling Pathways","description":"Protein glycosylation and phosphorylation play critical roles in regulating diverse cellular processes, yet their interplay remains underexplored. This study employed a dose-dependent glycosylation inhibition to investigate the function of glycosylation, especially in phosphorylation in epidermal growth factor (EGF) signaling. Using quantitative proteomics, we analyzed global protein expression, glycopeptides, and phosphopeptides in EGF-stimulated and unstimulated conditions. Results revealed that glycosylation inhibition disrupted phosphorylation patterns in EGF-regulated pathways. Notably, 215 EGF-regulated phosphopeptides exhibited dose-dependent changes, with pathways such as ERBB, MAPK, and mTOR signaling being significantly affected. Protein-protein interaction analysis highlighted glycosylation-dependent modulation of phosphorylation in cytoskeletal remodeling and growth factor signaling. Correlation analysis identified site-specific glycopeptides, such as Asn568 of EGFR, that influenced phosphorylation of downstream signaling proteins. Additionally, individual proteins like RCN1 and SLC4A7 demonstrated glycosylation and phosphorylation regulated patterns. These findings underscored the role of glycosylation in maintaining phosphorylation-dependent signaling fidelity, providing insights into function of glycosylation on cell signaling pathways.","dates":{"publication":"2026-04-06","submission":"2025-12-01"},"accession":"PXD071440","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:2042545","NEWT:148942","NEWT:193528","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:89187","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:57577","NEWT:156563","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:44270","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:93217","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:10031","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:109376","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:1190602","NEWT:3767","NEWT:433727","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:1176302","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:5535","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:143292","NEWT:2767842","NEWT:314345","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","NEWT:305400","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:160620","NCBITaxon:77643","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:32224","NEWT:11320","NEWT:1410384","NEWT:1310173","NEWT:1072569","NEWT:1072568","NEWT:161934","NEWT:156587","NEWT:1148","NEWT:5508","NEWT:135666","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1336794","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3710","NEWT:393133","NEWT:65125","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:32201","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:34875","NEWT:10882","NEWT:1431297","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:1423687","NEWT:657322","NEWT:10886","NEWT:3707","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:1301262","NEWT:319224","NEWT:2305479","NEWT:215451","NEWT:460519","NEWT:292415","NEWT:272843","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:223074","NEWT:2499525","NEWT:467144","NEWT:142786","NEWT:28196","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:387344","NEWT:657318","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:367737","NEWT:936350","NEWT:1883446","NEWT:380703","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:272831","NEWT:987059","NEWT:491","NEWT:422203","NEWT:460523","NEWT:2422","NEWT:2423","NEWT:3755","NEWT:85694","NEWT:85692","NEWT:911045","NEWT:3750","NEWT:175694","NEWT:1883456","NEWT:1195466","NEWT:2483192","NEWT:85698","NEWT:291146","NEWT:233271","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:34839","NEWT:476","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:1002697","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:427924","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:1120755","NEWT:1862567","NEWT:591090","NEWT:30455","NEWT:28141","NEWT:9030","NEWT:9031","NEWT:3728","NEWT:29471","NEWT:108931","NEWT:219799","NEWT:1325292","NEWT:219798","NEWT:548","NEWT:150475","NEWT:546","NEWT:1431340","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:451515","NEWT:8673","NEWT:630390","NEWT:550","NEWT:10804","NEWT:52694","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:40686","NEWT:1225786","NEWT:366497","NEWT:771870","NEWT:8665","NEWT:51338","NEWT:771875","NEWT:377142","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10835","NEWT:10832","NEWT:311339","NEWT:507601","NEWT:520","NEWT:64657","NEWT:186441","NEWT:2585209","NEWT:643680","NEWT:214092","NEWT:40697","NEWT:13095","NEWT:162425","NEWT:242124","NEWT:9986","NEWT:8654","NEWT:536","NEWT:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:480020","NEWT:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353154","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT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