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Weatheritt"],"technology_type":["Data-dependent acquisition","Affinity purification coupled with mass spectrometry proteomics","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Alternative splicing","Ap-ms","Lc-msms","Isoforms","Microexon"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD074758"],"tissue":["Cell Culture","Hela Cell"],"sample_protocol":["IP: We examined the protein interactomes of the SNX2 isoforms using affinity purification mass spectrometry (AP-MS) on HeLa wild type and HeLa SNX2 isoform rescue cell lines. HeLa cell lines were grown to 80-90% confluency in P150 dishes in supplemented DMEM with Pen/Strep. The cells were then washed 2x in ice cold 1xPBS, after which the cells were detached by cell scraping in 1mL 1xPBS. The detached cells were transferred to Eppendorf tubes and pelleted at 800 x g for 5min at +4°C. The supernatant was then removed, and the cell mass determined by weighing, and the cells were then snap frozen in LN2 and stored at -70°C. To immunoprecipitate SNX2 and interactors, the cell pellets were thawed on ice and then resuspended in immunoprecipitation buffer (20 mM HEPES pH 7.2, 100 mM K-acetate, 2.5 mM Mg-acetate, 0.1% Nonidet-P40 (NP40) (v/v), 1mM DTT, 10% glycerol (v/v)) at a ratio of 4µL/mg pellet by gentle pipetting. The cell suspensions was subjected to freeze-thaw to promote cell lysis. The lysates were then transferred to a tube spinner and spun at 12rpm for 30min at +4°C. The lysates were then transferred to a 2mL Dounce homogenizer for mechanical shearing (25 strokes). Homogenised lysates were transferred to Eppendorf tubes and spun at 17000 x g for 20min at +4°C to pellet nuclei/insoluble material. The supernatant was recovered and transferred to a new Eppendorf tube and mixed with 5µL anti-SNX2 antibody (BD Bioscience, Clone 13/SNX2), corresponding to 1.25µg antibody, and incubated on a tube spinner at 7rpm overnight at +4°C. The next day, the antibody-lysate mix was mixed with 50µL immunoprecipitation buffer-equilibrated Protein G Dynabeads Dynabeads (Thermo-Scientific), and the bead lysate suspension was incubated on a tube spinner at 7rpm for 2h at +4°C. Then, the suspension was put on a magnetic rack to pull down the bead-antigen-antibody complexes. The supernatant was removed, the tube was removed from the rack, and the beads were then resuspended in 1mL immunoprecipitation buffer and transferred to a new tube. The new tubes were placed on the magnetic rack and the supernatant was removed. The beads where then resuspended in 1mL wash buffer (20 mM HEPES pH 7.2, 10mM MgCl2) by gentle pipetting, and the tubes were placed on the magnet a final time and the supernatant was removed. The sample was then eluted from the beads by adding 30µL 4xLDS sample buffer diluted in 1xPBS with 20mM DTT. The sample was then incubated at +95°C for 5min, after which it was put back on magnet so the eluate could be isolated from the beads. Eluted samples were kept at -20°C until preparation for mass-spectrometry (within a week). Mass spectrometry sample prep: The IP eluates were first reduced with 5 mM DTT at 37 °C for 30 min, followed by alkylation with 10 mM iodoacetamide at room temperature in the dark for 30 min. Protein digestion was then performed using the SP3-based tryptic workflow (Christopher S. Hughes, et al., Single-pto, solid-phase-enhanced sample preparation for proteomics experiments. NATURE PROTOCOLS |VOL 14 |JANUARY 2019 | 68–85 |). Digested samples were desalted using two SDB-RPS disks (Empore, Sigma Cat#66886-U) packed into a 200 μL pipette tip. Extracted peptides from each clean-up were reconstituted in 10 μL 0.1% (v/v) formic acid, 0.05% (v/v) heptafluorobutyric acid and 2% acetonitrile in water.  Acquisition: Digest peptides were separated by nanoLC using an Ultimate nanoRSLC UPLC and autosampler system (Dionex, Amsterdam, Netherlands). Samples (2.5 µl) were concentrated and desalted onto a micro C18 precolumn (300 µm x 5 mm, Dionex) with H2O:CH3CN (98:2, 0.1 % TFA) at 15 µl/min. After a 4 min wash the pre-column was switched (Valco 10 port UPLC valve, Valco, Houston, TX) into line with a fritless nano column (75µ x ~30 cm) containing C18AQ media (1.9µ, 120 Å Dr Maisch, Ammerbuch-Entringen Germany). Peptides were eluted using a linear gradient of H2O:CH3CN (98:2, 0.1 % formic acid) to H2O:CH3CN (64:36, 0.1 % formic acid) at 200 nl/min over 90 min. High voltage 2000 V was applied to low volume Titanium union (Valco) and the tip positioned ~ 0.5 cm from the heated capillary (T=275°C) of a Orbitrap Fusion Lumos (Thermo Electron, Bremen, Germany) mass spectrometer. Positive ions were generated by electrospray and the Fusion Lumos operated in data dependent acquisition mode (DDA).  A survey scan m/z 350-1750 was acquired in the orbitrap (resolution = 120,000 at m/z 200, with an accumulation target value of 400,000 ions) and lockmass enabled (m/z 445.12003). Data-dependent tandem MS analysis was performed using a top-speed approach (cycle time of 2s). MS2 spectra were fragmented by HCD (NCE=30) activation mode and the ion-trap was selected as the mass analyzer. The intensity threshold for fragmentation was set to 25,000. A dynamic exclusion of 20 s was applied with a mass tolerance of 10ppm."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Data processing: Peak lists were generated using Mascot Daemon/Mascot Distiller (Matrix Science, London, England) using default parameters, and submitted to the database search program Mascot (version 2.8, Matrix Science). Search parameters were: Precursor tolerance 4 ppm and product ion tolerances ± 0.5 Da; Met (O) carboxyamidomethyl-Cys specified as variable modification, enzyme specificity was trypsin, 2 missed cleavage was possible and the Uniprot (February 2022, SProt_1_2_21.FASTA) was searched."],"omics_type":["Proteomics"],"labhead":["Robert J. Weatheritt"],"instrument_platform":[""],"submission_type":["COMPLETE"],"labhead_affiliation":["EMBL Australia, Garvan Institute of Medical Research, Darlinghurst, New South Wales, Australia. School of Biotechnology and Biomolecular Sciences, University of New South Wales, Sydney, New South Wales, Australia"],"species":["Homo Sapiens (human)"],"publication":["10.1101/2025.09.30.679652"],"submitter_mail":["r.weatheritt@garvan.org.au"],"submitter_affiliation":["UNSW Sydney"],"submitter_country":["Australia"],"doi":["10.6019/PXD074758"],"additional_accession":[]},"is_claimable":false,"name":"Examining protein interaction differences between sorting nexin 2 (SNX2) isoforms created by alternative splicing of a microexon exon, using AP-MS","description":"We examined how alternative RNA splicing affects protein interactions at large scale by creating a protein-protein interaction network using data from interaction databases and then examined how interactions might be affected by splicing. We also examined whether alternative RNA splicing often affected protein localisation within cells, which might come about from altered interactions. To do this, we created a targeted library of protein isoforms generated via alternative splicing events overlapping interfaces that mediate interactions, fused to fluorescent proteins. This library was transfected into HeLa cells and examined via high-content imaging. We found many protein isoforms that differed in the presence/absence of a cassette exon differed in localisation. A notable isoform pair detected in the imaging screen was two isoforms of sorting nexin 2 (SNX2) that differed in the inclusion/exclusion of 4-residues in SNX2’s BAR domain, which caused striking localisation differences. To examine this event further and examine potential connections to altered protein interactomes, we knocked out SNX2 in HeLa cells and rescued the knockout with either of the two SNX2 isoforms (untagged). We then used the rescue cell lines for affinity purification mass spectrometry (AP-MS) , using an antibody against SNX2, which recognize either isoform, for pulldown to identify potential differences in interactors. We didn’t find any clear evidence of different interactors for the two SNX2 isoforms, although noted both isoforms interacted with core SNX-BAR proteins, suggesting both isoforms form functional SNX-BAR complexes. We hypothesize that the lack of identified differential interactors may partly be due to loss of more transient interactors in our AP-MS approach. Accordingly, we found the two isoforms interacted differentially with the insulin receptor (INSR) in a LUMIER assay.","dates":{"publication":"2026-03-31","submission":"2026-02-24"},"accession":"PXD074758","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:2042546","NEWT:295546","NEWT:258594","NEWT:1126","NEWT:1129","NEWT:309807","NEWT:89184","NEWT:309800","NEWT:1323429","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:10034","NEWT:661410","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:3767","NEWT:135622","NEWT:672127","NEWT:656061","NEWT:37965","NEWT:656064","NEWT:3760","NEWT:36630","NEWT:381198","NEWT:418106","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:44250","NEWT:317447","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:12637","NEWT:2164133","NEWT:2767846","NEWT:314344","NEWT:108061","NEWT:224308","NEWT:49928","NEWT:160621","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:1230383","NEWT:77133","NEWT:1310165","NEWT:114727","NEWT:5516","NEWT:498211","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:1310173","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:419481","NEWT:5507","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:1143","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:709964","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:1616117","NEWT:34865","NEWT:550537","NEWT:284812","NEWT:3701","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:1246791","NEWT:9005","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:1883426","NEWT:657321","NEWT:10886","NEWT:3708","NEWT:536231","NEWT:219813","NEWT:215451","NEWT:460519","NEWT:272844","NEWT:1348799","NEWT:55784","NEWT:485","NEWT:2499525","NEWT:142786","NEWT:2853422","NEWT:487","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:216778","NEWT:376686","NEWT:237610","EFO:0001352","NEWT:219809","NEWT:219808","NEWT:119562","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:141469","NEWT:987059","NEWT:491","NEWT:460523","NEWT:85694","NEWT:85692","NEWT:3750","NEWT:291146","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:278161","NEWT:415978","NEWT:410289","NEWT:191701","NEWT:9054","NEWT:472","NEWT:29459","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:445","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:215402","NEWT:3726","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:3728","NEWT:108931","NEWT:219799","NEWT:219798","NEWT:548","NEWT:150475","NEWT:256737","NEWT:51350","NEWT:8694","NEWT:8692","NEWT:542","NEWT:394503","NEWT:13076","NEWT:219785","NEWT:8673","NEWT:550","NEWT:10804","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:42410","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:9995","NEWT:28112","NEWT:49012","NEWT:28110","NEWT:10832","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:8658","NEWT:1268063","NEWT:8657","NEWT:9983","NEWT:8655","NEWT:80833","NEWT:479096","NEWT:28108","NEWT:28104","NEWT:1114957","NEWT:568703","NEWT:568708","NEWT:52641","NEWT:353152","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NCBITaxon:1763","NEWT:443906","NEWT:13037","NEWT:519","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:300641","NEWT:39655","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697","NEWT:861109","NEWT:8695","NEWT:1196866","NEWT:1045775","NEWT:1123869","NCBITaxon:1335626","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:27697","NEWT:86185","NEWT:9935","NEWT:287889","NEWT:1028307","NEWT:52603","NEWT:92867","NEWT:92866","NEWT:1344414","NEWT:202950","NEWT:741158","NEWT:1293091","NEWT:202956","NEWT:315750","NEWT:632957","NEWT:9925","NCBITaxon:9606","NEWT:1436183","NEWT:4232","NEWT:9922","NEWT:416348","NEWT:11298","NEWT:4236","NEWT:398031","NEWT:196627","NEWT:523840","NEWT:1076878","NEWT:200308","NEWT:200302","NEWT:9913","NEWT:9915","NEWT:105841","NEWT:2666255","NEWT:999810","NEWT:28995","NEWT:1392998","NEWT:1150621","NEWT:1085791","NEWT:745531","NEWT:226900","NEWT:231490","NEWT:590651","NEWT:449239","NEWT:244704","NEWT:9909","NEWT:9902","NEWT:430615","NEWT:563041","NEWT:36599","NEWT:41949","NEWT:326423","NEWT:326424","NEWT:13013","NEWT:749906","NEWT:418985","NEWT:749907","NEWT:431947","NEWT:142809","NEWT:1095183","NEWT:302409","NEWT:9979","NEWT:130821","NEWT:2320211","NEWT:27606","NEWT:290610","NEWT:1519788","NEWT:59202","NEWT:9975","NEWT:8643","NEWT:1801631","NEWT:1159899","NEWT:502780","NEWT:860688","NEWT:35231","NEWT:1774208","NEWT:8644","NEWT:1125630","NEWT:202914","NEWT:222523","NEWT:27602","NEWT:502779","NEWT:297246","NEWT:483139","NEWT:101491","NEWT:8639","NEWT:8637","NEWT:1114970","NEWT:285272","NEWT:192222","NEWT:9963","NEWT:197911","NEWT:197912",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