{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Xlsx":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Sample_Matrix_supplement.xlsx"],"Msf":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07238_C2C12_Scr_secretomics_Pellet_N-1.msf"],"Txt":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/checksum.txt"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07854_C2C12_Scramble_Secretomics_Set_6_Aug_21st_2023.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07856_C2C12_sh6FPH_2_Set_5_Secretomic_Analysis_Aug_18th_2023.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07244_C2C12_shGFPT1_2_Pellet_Set_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07243_C2C12_shGFPT1_1_Pellet_Set_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07862_C2C12_sh6FPH_1_Set_3_Secretomic_Analysis_Aug_18th_2023.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07857_C2C12_sh6FPH_2_Set_1_Secretomic_Analysis_Aug_18th_2023.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07869_C2C12_sh6FPH_1_Set_5_Secretomic_Analysis_Aug_18th_2023.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07859_C2C12_Secretomics_Supernatant_Set_1_Scramble.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07240_C2C12_Scr_secretomics_Pellet_N-3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07246_C2C12_shGFPT1_2_Pellect_Set_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07242_C2C12_shGFPT1_1_Pellet_Set_5.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07867_C2C12_sh6FPH_2_Set_3_Secretomic_Analysis_Aug_18th_2023.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07871_C2C12_sh6FPH_1_Set_4_Secretomic_Analysis_Aug_18th_2023.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07861_C2C12_Secretomics_Supernatant_Set_2_Scramble.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07241_C2C12_shGFPT1_1_Pellet_Set_3.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07245_C2C12_shGFPT1_2_Pellet_Set_4.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07239_C2C12_Scr_secretomics_Pellet_N-2.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/Std-QExactive01-07238_C2C12_Scr_secretomics_Pellet_N-1.raw"],"Other":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/08/PXD079191/20250514_100355_aH_C2C12_secretome_sh6FPH_Holland_Ottawa.sne"]},"type":"primary"},"statusCodeValue":200,"statusCode":"OK"}],"scores":null,"additional":{"labhead_mail":["albert.sickmann@isas.de"],"submitter":["Andreas Hentschel"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics","Data-independent acquisition"],"software":[""],"submitter_keywords":["Congenital myasthenic syndrome","Trafficking","Gfpt1","Autophagy"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD079191"],"tissue":["Cell Culture"],"sample_protocol":["Gfpt1-deficient and scramble cells were seeded into separate 15 cm plates. At 75% confluency Gfpt1 silencing was achieved by doxycycline treatment at 2 μg/mL for 72 hours. (Sigma, D9891). Prior to collection of cells were serum starved for three hours, followed by a replacement with growth media for one hour, and finally serum starved for 4 hours. Conditioned media was collected, centrifuged at 1,000 x g for 15 minutes. Supernatant was collected and snap frozen. This sample was represented as the secretome.  Frozen cell pellets were treated with 200 µL of lysis buffer (50 mM TEAB, pH 7.8, 5% SDS, supplemented with cOmplete™ ULTRA protease inhibitor cocktail, Roche), followed by mechanical disruption using a Bioruptor® sonication system (Diagenode) for 10 min (30 s on/30 s off, 10 cycles) at 4 °C. To achieve complete homogenization, samples were additionally subjected to probe sonication (30 s, 1 s on/1 s off, amplitude 40%), and insoluble material was removed by centrifugation (20,000 × g, 15 min, 4 °C). Protein concentration in the cleared supernatant was quantified using the BCA assay according to the manufacturer’s instructions. Reduction of disulfide bonds was performed by incubation with 10 mM TCEP at 37 °C for 30 min, followed by alkylation with 15 mM IAA at room temperature for 30 min in the dark. For proteolytic digestion, 100 µg of total protein from each sample was processed using the S-Trap protocol (Protifi) with a protein-to-trypsin ratio of 20:1. Digestion was carried out for 2 h at 42 °C, and the reaction was terminated by acidification with formic acid to a final pH below 3. The completeness of proteolytic cleavage was evaluated following desalting by monolithic column separation (PepSwift PS-DVB PL-CAP200-PM, Dionex) using an UltiMate 3000 HPLC system (Dionex, Germering, Germany). For each analysis, 1 µg of digest was injected directly. Chromatographic separation was achieved with a binary gradient (solvent A: 0.1% TFA; solvent B: 0.08% TFA in 84% acetonitrile), starting at 5–12% B over 5 min, followed by 12–50% B over 15 min, at a flow rate of 2.2 µL/min and 60 °C. UV detection was carried out at 214 nm.  Scramble and Gfpt1-deficient C2C12 myoblasts were seeded into 10 cm plates. At 75% confluency, growth medium was changed into serum free medium for four hours, then growth medium was applied for an hour, followed by another three hour incubation with starvation medium. Media was collected and centrifuged to remove cell debris and snap frozen in 10 mL aliquots for proteomic analysis.   Each sample was divided into two aliquots of 1 mL cultured medium. Protein precipitation was carried out by adding 3 mL of ice-cold acetone to each aliquot, followed by incubation overnight at -20 oC. Subsequently, the samples were centrifuged at 20,000 x g for 20 minutes at 4oC to pellet the proteins. The acetone supernatant was carefully removed, and the pellets were air dried for 3 to 5 minutes. To bring the protein pellets into solution, 100 μL lysis buffer (50 mM TEAB, pH 7.8; 5% SDS; and cOmplete ULTRA protease inhibitor, Roche) was added to each sample. Complete lysis was ensured using a Bioruptor® (Diagenode) for 10 minutes at 4 °C (30-second cycles of sonication and rest, 10 cycles total). Finally, the aliquots were combined to reconstitute the original sample. Reduction of disulfide bonds was performed by incubation with 10 mM TCEP at 37 °C for 30 min, followed by alkylation with 15 mM IAA at room temperature for 30 min in the dark. For proteolytic digestion, 100 µg of total protein from each sample was processed using the S-Trap protocol (Protifi) with a protein-to-trypsin ratio of 20:1. Digestion was carried out for 2 h at 42 °C, and the reaction was terminated by acidification with formic acid to a final pH below 3."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For the analysis of the samples acquired with nano-LC-MS/MS in DIA mode, the data was introduced to the Spectronaut software (Biognosys) and analyzed with a direct DIA-based search. As library the mouse proteome data was selected from UniProt (www.uniprot.org) containing 17,175 entries (downloaded on August 23rd 2023). Search and extraction settings were kept as standard (BGS Factory settings) Normalization was done by the software, using global normalization based on the median. For reliable label-free quantification, only proteins identified with ≥ 2 unique peptides were considered for further analysis. Subsequently, the average normalized abundances (determined using Spectronaut) were calculated for each protein and used to determine the ratio between the leukocytes from the patients and the corresponding controls. Finally, a Student's t-test with p-values was calculated in MS Excel. Only proteins with a p-value of ≤0.05 and an abundance ratio of ≥2 or ≥0.5 (up-regulated as well as down-regulated) were considered as finally regulated.  All MS raw data underwent processing using Proteome Discoverer software version 2.5.0.400 (Thermo Scientific, Bremen, Germany) and were subjected to a target/decoy mode search against a mouse Uniprot database (www.uniprot.org, downloaded on 08 October 2019) utilizing the MASCOT and Sequest algorithm. The search parameters included precursor and fragment ion tolerances of 10 ppm and 0.02 Da for MS and MS/MS, respectively. Trypsin was designated as the enzyme with a maximum of 2 allowed missed cleavages. Carbamidomethylation of cysteine was set as a fixed modification, and oxidation of methionine was set as a dynamic modification. Percolator false discovery rate (strict) was established at 0.01 for both peptide and protein identification. The statistical analysis in regard for significance and up- or downregulated proteins was conducted as described above."],"omics_type":["Proteomics"],"labhead":["Prof. Dr. Albert Sickmann"],"instrument_platform":[""],"labhead_affiliation":["Proteomics, Leibniz-Institut für analytische Wissenschaften -ISAS - e.V., Germany"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["andreas.hentschel@isas.de"],"publication":["10.3390/BIOM16070966"],"submitter_affiliation":["Leibniz Institut für Analytische Wissenschaften"],"submitter_country":["Germany"],"additional_accession":[]},"is_claimable":false,"name":"Hexosamine Pathway Disruption by GFPT1 Loss Drives Coordinated Defects in Glycosylation, Autophagy, and Trafficking","description":"Gfpt1, the rate limiting enzyme of the hexosamine biosynthetic pathway (HBP), provides the UDP-GlcNAc required for protein glycosylation. Biallelic mutations in GFPT1 cause congenital myasthenic syndromes (GFPT1-CMS), yet the molecular mechanisms linking impaired glycosylation to skeletal muscle dysfunction remain incompletely understood. Here, we combine cellular models of inducible Gfpt1 knockdown and a muscle-specific Gfpt1 knockout mouse (Gfpt1Tm1d/Tm1d) with whole-cell proteomics, immunoblot studies and secretomics to define glycosylation-dependent defects in intracellular trafficking, ER stress signaling and autophagy. Global proteomic profiling of Gfpt1-deficient myoblasts revealed marked downregulation of protein trafficking pathways and impaired secretion of key muscle cargo proteins, including Srgn. Loss of GFPT1 reduced both high–molecular weight glycosylated SRGN and its core protein, accompanied by intracellular retention and decreased secretion. These trafficking defects coincided with robust activation of the unfolded protein response (UPR), evidenced by increased Xbp1 expression and accumulation of spliced Xbp1s across pharmacologic, cellular, and mouse models of GFPT1 deficiency. Converging evidence from proteomics, immunoblotting, and immunofluorescence demonstrated impaired autophagy, including increased LC3 II accumulation, elevated p62/SQSTM1 levels, and enhanced p62 positive puncta in both myoblasts and Gfpt1-deficient skeletal muscle. Soluble/insoluble fractionation further confirmed p62 accumulation, indicating defective autophagic flux and buildup of aggregated cargo. Together, these findings identify a glycosylation dependent failure in protein trafficking that triggers ER stress, UPR activation, and autophagy impairment in Gfpt1-deficient skeletal muscle. This mechanistic cascade provides a unifying explanation for muscle pathology in GFPT1 associated congenital myasthenic syndromes and suggests that restoring glycosylation or improving proteostasis may represent viable therapeutic approaches.","dates":{"publication":"2026-08-04","submission":"2026-06-02"},"accession":"PXD079191","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:111205","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:383379","NEWT:418106","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: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: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: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:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2709072","NEWT:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:294607","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:109760","NEWT:29031","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:108458","NEWT:5936","NEWT:320637","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","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","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:8655","NEWT:5147","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:40674","NEWT:1194669","NEWT:51329","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","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:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:305959","NEWT:13489","NEWT:92867","NEWT:92866","NCBITaxon:3055","NEWT:51750","NEWT:202950","NEWT:295027","NCBITaxon:11320","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:90690","NEWT:1436183","NEWT:4232","NEWT:416348","NEWT:11298","NEWT:7742","NEWT:196627","NEWT:200308","NEWT:200302","NEWT:870435","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NCBITaxon:5693","NEWT:28995","NEWT:1392998","NEWT:380394","NEWT:226900","NEWT:1266738","NEWT:231490","NEWT:244704","NEWT:7725","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:72664","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:452467","NEWT:198822","NEWT:36111","NEWT:326424","NEWT:1678078","NEWT: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