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Parker"],"technology_type":["Mass Spectrometry","Chemical cross-linking coupled with mass spectrometry proteomics"],"software":["Not available"],"submitter_keywords":["Mouse skeletal muscle","Insulin resistance"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD077541"],"tissue":["Extensor Digitorum Longus"],"sample_protocol":["Subcellular fractionation of C2C12 myotubes and EDL muscles was performed using a Subcellular Fractionation Kit (Thermo Scientific; 87790) according to their product protocol. Resulting fractions were precipitated with chloroform/methanol and digested with trypsin at a 1:50 enzyme:substrate ratio.  Resulting fractions were labelled with isobaric tags for quantification. Every 1 µg of peptide was labelled with 2 µg of 16-plex tandem mass tags (TMTpro) in 50% acetonitrile at room temperature for 1.5 h (Zecha et al., 2019). The reaction was deacylated with 0.3% (w/v) of hydroxylamine for 10 min at room temperature and quenched to a final volume of 0.1% formic acid (FA) and <5% acetonitrile and pooled. Pooled fractions (4 total) were then loaded onto a HLB-SPE column (Waters Corp; #186008055) pre-conditioned with 1 ml of methanol followed by 1 ml of acetonitrile and finally 2 ml of 0.1% FA. Columns were washed with 2 ml of 0.1% FA and eluted with 1 ml of 80% acetonitrile, 0.1% FA. Phosphopeptides were pre-cleared with 10ul of Fe-NTA Magnetic Agarose beads (Thermo Scientific; A52284) per 500 µg of peptide pre-washed with 1 ml of 80% acetonitrile, 0.1% FA. The unbound flowthrough which contained our protected cross-linked and regular peptides were collected and dried down in a Speedvac at 45 degrees Celsius. The cross-linked/regular peptide flowthrough was resuspended in 100 µl of 0.5% TFA and bath sonicated for 5 minutes. Samples were then shaken at room temperature for 2 hours at 1,800 RPM which deprotected cross-linked peptides. Each sample was diluted to a final concentration of 80% acetonitrile and 0.1% TFA with 400 µl of acetonitrile and transferred to another lo bind tube containing 10ul of Fe-NTA Magnetic Agarose beads (Thermo Scientific; A52284) per 500 µg of peptide pre-washed with 1 ml of 80% acetonitrile, 0.1% TFA. Samples were shaken again for 30 minutes at room temperature at 1,800 RPM to bind deprotected PhoX-modified peptides, after which the unbound flowthrough containing regular peptides only (total proteome) was collected and saved. Beads were washed with 1 ml 80% acetonitrile and 0.1% TFA three times and saved. PhoX-modified peptides were then eluted off the beads twice with 100 µl of 5% ammonium hydroxide shaken at 2000 RPM for 2 minutes at room temperature. The PhoX-modified peptide eluates, as well as regular non-modified peptide fractions for global total proteomic analysis were then loaded onto in-house packed C8 microcolumns to remove any trace agrose beads (3M Empore; #11913614) and centrifuged at 1,000 g and collected in PCR strip tubes. C8 microcolumns were washed with 5 µl of 50% acetonitrile and collected into the same tube to ensure no remaining peptides in the column. Samples were then dried to approximately 50 µl in a Speedvac at 45°C and 200 µl of 99% isopropanol, 1% TFA was added. Peptides were purified by in-house packed SDB-RPS (Sigma; #66886-U) microcolumns and dried by vacuum centrifugation. The PhoX-modified peptides were resuspended in 30% acetonitrile, 0.1% TFA while the non-modified peptides were resuspended in 2% acetonitrile in 0.1% TFA and all samples were stored at -80°C. PhoX-modified peptides were subjected to size exclusion chromatography (SEC) separation as previously described (Harney & Larance, 2023) and 2-3 fractions further separated by by neutral phase C18BEH HPLC into 12 fractions."],"repository":["Pride"],"quantification_method":["Not available"],"modification":[""],"data_protocol":["For XL-MS, peptides were analysed on a Dionex 3500 nanoHPLC, coupled to an Orbitrap Eclipse mass spectrometer (ThermoFischer Scientific) via electrospray ionization in positive mode with 1.9 kV at 275 °C and RF set to 30%. Separation was achieved on a 50 cm × 75 µm column packed with C18AQ (1.9 µm; Dr Maisch, Ammerbuch, Germany) (PepSep, Marslev, Denmark) over 20 or 60 min depending on the offline fractionation UV trace at a flow rate of 300 nL/min. The peptides were eluted over a linear gradient of 3–40% Buffer B (Buffer A: 0.1% v/v formic acid; Buffer B: 80% v/v acetonitrile, 0.1% v/v FA) and the column was maintained at 50 °C. The instrument was operated in data-dependent acquisition mode with an MS1 spectrum acquired over the mass range 350–2000 m/z (60,000 resolution, 200% automatic gain control (AGC) and 50 ms maximum injection time) followed by MS/MS via HCD fragmentation with a cycle time of 3 seconds where only peptides with charge state 3-8 were selected with 1.2 m/z isolation window (30,000 resolution, stepped collision energy of 35±8%, 200% AGC, maximum injection time set to 110 ms, enhanced TMTPro resolution mode). XL-MS data were searched against the same skeletal muscle mouse specific proteome database with pLink2 (v2.3.11, Chen et al., 2019). The peptides were searched with oxidation of methionine set as variable modification, and carbamidomethylation of cysteine and TMT to peptide N-termini and Lysine set as a fixed modification set as a fixed modification. Default parameters were used with up to 2 missed cleavages allowed, filter tolerance was set to 10 ppm and peptides were filtered to 1% FDR. XL-MS search was performed using tBu-PhoX as the set linker, where elemental composition was manually imported using cross-linker information from ProteomeDiscoverer."],"omics_type":["Proteomics"],"labhead":["Benjamin Parker"],"instrument_platform":[""],"labhead_affiliation":["The University of Melbourne"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["ben.parker@unimelb.edu.au"],"publication":["Not available"],"submitter_affiliation":["The University of Melbourne"],"submitter_country":["Australia"],"additional_accession":[]},"is_claimable":false,"name":"qXL-MS of insulin resistance in mouse skeletal muscle","description":"We established a whole tissue qXL-MS workflow to investigate proteome-wide changes in protein:protein interactions in mouse skeletal muscle insulin resistance (IR). Mice were feed a standard chow diet or a high fat diet (HFD) for 12 weeks which induced skeletal muscle insulin resistance. The Extensor digitorum longus (EDL) skeletal muscles were isolated and subjected to qXL-MS analysis. We chose this small fast-twitch muscle because it weighs ~8-10 mg providing sufficient protein yield (~1 mg) and it is commonly used in ex vivo myograph preparations due to adequate oxygen diffusion in O2/CO2-carbogen gassed Krebs-Henseleit bicarbonate-based buffer (Barclay, 2005). For XL-MS analysis of IR in skeletal muscle, chow and HFD EDL muscles (n=8 each) were incubated with 10 mM tPhoX for 2h.","dates":{"publication":"2026-05-29","submission":"2026-04-23"},"accession":"PXD077541","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: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:317447","NEWT:4688","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:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","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:2853422","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","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","NCBITaxon:2","NEWT:568708","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:40674","NEWT:1194669","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:72664","NEWT:563041","NEWT:41949","NEWT:326423","NEWT:452467","NEWT:198822","NEWT:36111","NEWT:326424","NEWT:1678078","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:150847","NEWT:431947","NEWT:69014","NEWT:142809","NEWT:302409","NEWT:130821","NEWT:27606","NEWT:1519788",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