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Xu"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Alternative splicing","Transcriptomics","Tandem mass tags (tmt)","Proteome"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD068593"],"tissue":["Whole Body"],"sample_protocol":["Arabidopsis thaliana Col-0 (WT) and acinus-2 pinin-1 (ap) mutants  (Bi et al., 2021, Nat Commun) were used. Seeds were surface-sterilized, stratified for 3 days, and germinated on ½ MS agar plates at 22 °C under constant light. Seedlings were harvested at specific stages. Plates were grown vertically. Tissue (100 mg) from 9-day-old wild-type and acinus pinin seedlings grown on vertical plates was harvested, flash-frozen, and ground. Proteins were extracted as described in (Xu et al., 2017, PNAS), with a slight modification to extraction buffer Y (100 mM Tris-HCl, pH 8.0; 2% SDS w/v; 5 mM EGTA; 10 mM EDTA; 1 mM PMSF; 2× protease inhibitor, Roche). Extracts were reduced with TCEP, alkylated, and digested with trypsin, followed by desalting using Sep-Pak columns (Waters).  TMT 11-plex reagents (ThermoFisher, Cat# A34808) were reconstituted in anhydrous acetonitrile (0.01 mg/μL). Approximately 200 μg of peptides from each sample were dissolved in 66 μL of 50 mM HEPES buffer. Of this, 60 μL (182 μg) was labeled with 40 μL of TMT reagents (TMT126–130N), while the remaining 6 μL (18.2 μg) was pooled to 60 μL and labeled with 40 μL TMT131C. Reactions proceeded for 1 h at 25 °C with shaking at 700 rpm and were quenched with 5 μL of 1 M Tris (pH 8). Peptides were then acidified with 45 μL of 10% FA in 10% acetonitrile. The final reaction contained TMT at 4 μg/μL, peptides at 2 μg/μL, and 40% acetonitrile (v/v)  (Zecha et al., 2019, MCP). The labeling scheme is shown in Supplementary Figure 3. One-eighth of the 11 labeled samples was combined for high-pH reversed-phase HPLC fractionation (Xu et al., 2017, PNAS). High pH reverse-phase chromatography was performed on the Vanquish Flex system (ThermoFisher) equipped with a 4.6×150-mm Gemini 5μm C18 column for TMT-labeled peptides and AspN digested samples. Peptides were loaded onto the column in 25 μL of buffer A (20 mM ammonium formate, pH 10). Buffer B consisted of buffer A with 90% (vol/vol) acetonitrile. Peptides were separated at 0.5 mL/min using high-pH reversed-phase gradients. Common steps included column equilibration at 1% B and sequential increases to 50–70% B, 70–100% B, and 100% B hold. Fraction were collected every 1–2 min. TMT batch 2: 10 min equilibration; 1–10% B in 10 min, 10–50% B in 40 min; fractions every 2 min. TMT Batch 3: 10 min equilibration; 1–10% B in 20 min, 10–50% B in 80 min; fractions every 1 min. Collected fractions were vacuum-dried and subjected to LC/MS/MS analysis. Peptides were analyzed on a Orbitrap Eclipse hybrid quadrupole-Orbitrap mass spectrometer (Thermo Fisher) coupled to an Easy LC 1200 UPLC system. Peptides were trapped on an Acclaim PepMap 100 C18 column (75 μm × 2 cm) and separated on a 25 cm × 75 μm, 1.7 μm C18 Aurora column (IonOpticks) at 300 nL/min using a 120 min gradient: 3–28% solvent B (80% ACN, 0.1% FA) over 106 min, 28–44% B over 15 min, followed by a 9 min wash at 90% B. Batch 2 and 3 TMT samples were analyzed on the Eclipse; TMT samples were measured using real-time library search (Furtwangler el al., 2022, MCP), with MS1 m/z 400–1600, resolution 120,000, intensity threshold 5E3, charge 2–6, dynamic exclusion 45 s; MS2 in the ion trap (isolation 0.7 m/z, CID 35%, max injection 35 ms); MS3 using synchronous precursor selection of 10 precursors (isolation 0.7 m/z, HCD 65%, Orbitrap resolution 50,000, scan range 100–500 m/z, max injection 200 ms, cycle time 2.5 s). Real-time data searches were performed against the TAIR10 database with carbamidomethyl and TMT11plex (static) and oxidation (variable) modifications."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["For Isoform-specific peptides both batch 2 and batch 3 searched using Protein Prospector and MSFragger with similar parameters. For both software, the precursor mass tolerance was set to 10 ppm and MS/MS tolerance to 20 ppm. Carbamidomethylation of cysteine was set as a fixed modification, while variable modifications included protein N-terminal acetylation, peptide N-terminal Gln conversion to pyroglutamate, and methionine oxidation. Cleavage specificity was set to AspN, allowing one missed cleavage and up to two modifications per peptide. Raw data were searched against the Araport11 protein database, which contains 48,354 entries. False discovery rates (FDR) were set at 5% for proteins and 1% for peptides. For TMT quantification only batch 3 was used. Raw files were searched using MaxQuant v2.4.2.0. In the global parameters, the type was set to MS3 ion reporter mode using the correction factors provided by the TMT reagents. No normalization setting was set. The first peptide mass tolerance was set to 20 ppm and the main search peptide mass tolerance was set to 4.6 ppm.  The MS2 match tolerance was set to 20 ppm. Reporter mass tolerance was set to 0.003, and the isobaric weight exponent was set to 0.75. The reference protein database used was a modified version of the Arabidopsis Thaliana TAIR 10 database, downloaded from TAIR: “TAIR10_pep_20101214.fa”. All other parameters remained at their default. For protein level analysis: MaxQuant outputs proteinGroups.txt and evidence.txt were used with R package MStatsTMT (Huang, et al., 2020, MCP). The parameters for MSstatsTMT’s proteinSummarization function: method was set to msstats, global normalization was set to true, reference normalization was set to true, and remove normalization channel was set to true. Protein level quantifications for each sample were analysed to impute protein quantifications that were only completely missing in one condition. The impute was done from a normal distribution with a width of 0.3 and downshifted 1.8 from the values of the total matrix. Following imputation, a moderated statistics test was done using MSstatsTMT’s groupComparisonTMT function. Proteins with missing p-values were filtered out. If an ambiguous protein group existed with different gene loci, they were discarded. If multiple protein groups existed for a single gene locus, the protein group with the most peptides quantified was kept. Protein groups with a p-value less than or equal to 0.05 and a fold change greater than or equal to 1 or less or equal to -1 were considered as differentially abundant proteins. Peptide level quantifications shown in Figure 5G were generated from Maxquants’s peptides.txt output. To determine each peptide’s position relative to intronic regions, we developed a custom R script that maps intron coordinates onto specific isoforms."],"omics_type":["Proteomics"],"labhead":["Shouling Xu"],"instrument_platform":[""],"labhead_affiliation":["Department of Plant Biology, Carnegie Institution for Science, Stanford, California, USA"],"submission_type":["PARTIAL"],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"publication":["42080264 Reyes AV, Zhang C, Karunadasa SS, Shrestha R, Grismer TS, Byun D, Xu SL. Impact of alternative splicing on Arabidopsis proteome. Nucleic Acids Res. 2026 54(8):gkag400 10.1093/nar/gkag400"],"submitter_mail":["sxu@ciw.edu"],"submitter_affiliation":["Carnegie Institution at Stanford"],"submitter_country":["United States"],"pubmed_abstract":["Limited proteomic evidence makes it unclear to what extent alternative splicing (AS) isoforms are translated and functionally relevant in eukaryotes. Here, we present a comprehensive proteomic analysis in plants using large-scale data mining, extensive fractionation of AspN- and trypsin-digested proteomes, and both label-free and TMT labeling. In total, we identified 471 196 peptides from 22 479 proteins by searching against Araport11, revealing 32 110 isoform-specific peptides. Using an integrated proteogenomic workflow coupled with SUPPA, we classified these peptides into 2442 AS events, 879 of which involved intron retention (IR). Further analysis of unannotated events revealed 91 additional IRs that are translated, supporting that retained introns can give rise to peptides. AlphaFold modeling predicted the structural and functional impacts of these isoforms. Our dataset improved existing gene model annotations. By comparing wild-type plants with the AS mutant acinus pinin, we found that IR regulates transcript and protein abundance nonlinearly. Phenotypic assays revealed the functional consequences, including reduced chlorophyll, impaired growth, and increased anthocyanin. Overall, our results support widespread translation of AS isoforms in plants and suggest that AS contributes to proteome diversification, protein abundance regulation, and growth and developmental outcomes."],"pubmed_title":["Impact of alternative splicing on Arabidopsis proteome."],"pubmed_authors":["Reyes Andres V AV, Zhang Christopher C, Karunadasa Sumudu S SS, Shrestha Ruben R, Grismer TaraBryn S TS, Byun Danbi D, Xu Shou-Ling SL"],"additional_accession":[]},"is_claimable":false,"name":"Impact of alternative splicing on Arabidopsis proteome (Part III, TMT RT-SPS-MS3)","description":"Alternative splicing (AS) is a key regulatory process in eukaryotes. Despite its importance, the impact of AS on plant protein diversity and its global effect on the proteome remain largely unexplored. To address this, we included the AS acinus pinin mutant in our qualitative proteomic analysis to identify splice variants, and in our quantitative analysis to assess the impact of intron retention (IR) on protein abundance. Specifically, we (1) investigated global proteomic changes in acinus pinin double mutants using tandem mass tag (TMT) labeling. ACINUS and PININ are evolutionarily conserved splicing factors, and their disruption induces splicing events resembling those triggered by various stressors. We employed TMT labeling with real-time search MS3 (RTS-SPS-MS3), combined with extensive sample fractionation, to maximize proteome coverage and achieve accurate quantification. (2) To enhance isoform-specific peptide detection, we incorporated data generated using the alternative protease AspN, along with mined data from the Arabidopsis Proteome Draft (Mergner et al., 2020, Nature). This TMT-based approach allowed us to assess how increased intron retention (IIR) affects the proteome by integrating proteomic data with matched transcriptomic profiles. Moreover, our method enabled identification of isoform-specific peptides—both annotated and previously unannotated—using in-house algorithms and filtering steps. These findings demonstrate that alternatively spliced transcripts are translated and detectable at the protein level, providing insight into the functional consequences of isoform diversity and revealing the complex relationship between AS and protein abundance.","dates":{"publication":"2026-06-08","submission":"2025-09-19"},"accession":"PXD068593","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","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:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","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:2492962","NEWT:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:1177","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:143292","NEWT:224308","NEWT:3134131","NEWT:49928","NEWT:160621","NEWT:110368","NCBITaxon:5204","NEWT:1916073","NEWT:1303873","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: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:3712","NEWT:3711","NEWT:3714","NEWT:65121","NEWT:3716","NEWT:3715","NEWT:2065263","NEWT:1549675","NEWT:177437","NEWT:9014","NEWT:10891","NEWT:118221","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:28174","NEWT:550537","NEWT:284812","NEWT:284811","NEWT:2902907","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: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:1883446","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:123606","NEWT:1195466","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:1380096","NEWT:28128","NEWT:470","NEWT:41122","NEWT:1328300","NEWT:748693","NEWT:106299","NCBITaxon:50557","NEWT:63363","NEWT:3735","NEWT:29491","NEWT:911022","NEWT:446","NEWT:153481","NEWT:714485","NEWT:445","NEWT:2003758","NEWT:29486","NEWT:63366","NEWT:64697","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: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: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: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:51315","NEWT:52641","NEWT:353152","NEWT:116597","NEWT:353153","NEWT:116598","NEWT:227377","NEWT:1774284","NEWT:27689","NEWT:207769","NEWT:40674","NEWT:51329","NCBITaxon:1763","NEWT:443906","NEWT:6055","NEWT:13037","NEWT:518","NEWT:519","NEWT:941638","NEWT:511","NEWT:7394","NEWT:6063","NEWT:404330","NEWT:1328388","NEWT:13064","NEWT:529120","NEWT:7375","NEWT:300641","NEWT:39655","NEWT:38323","NEWT:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:52638","NEWT:8697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