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Lyons"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Plant","Phosphorylation","Endomembrane system","Stomata","Vacuole","Guard cell"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD070005"],"sample_protocol":["Protein sample preparation Samples were ground in mortar and pestle with liquid nitrogen and protein was extracted in a lysis buffer consisting of 8M urea (Thermo Fisher 29700) in 50 mM Tris-HCl (VWR 97061-794) pH 7.8, 1x cOmplete™ EDTA-free Protease Inhibitor Cocktail (Sigma-Aldrich 11836170001) and 1x Pierce™ Phosphatase Inhibitor Mini Tablets cocktail (Thermo Fisher A32957).  Samples were incubated on ice for 10 minutes, gently vortexed, and centrifuged at 8,000 × g at 4 ºC for 10 minutes. The supernatant was further cleared by centrifugation at 12,000 × g at 4 ºC for 5 minutes. The final supernatant for each condition was mixed to maximize total protein concentration and evenly divided between three technical replicates per condition (open or closed) and flash frozen. To measure total protein concentration, a small amount of each sample was aliquoted and used in a Bradford assay (AlfaAesar VWR AAJ61522-AP). Protein extraction from the frozen samples was conducted for all samples together on one day. Each sample was acetone precipitated, then pellets were reconstituted in 1M Urea and processed. Samples were  reduced with 5mM Dithiothreitol (Thermo Fisher 20290) for 45 minutes at 37 ºC, alkylated with 15 mM iodoacetamide (Thermo Fisher A39271) for 30 minutes in the dark at room temperature. Samples were then digested with LysC (Wako, VWR 125-02543 1:50 w/w) for 2 hours at 37°C, followed by overnight trypsin (Sequencing Grade, Promega V5111, 1:50 w/w) digestion at 37°C. The resulting peptide samples were acidified and desalted using desalting spin columns (Thermo Fisher 89852), and the eluates were dried via vacuum centrifugation. Peptide concentration was determined using Pierce Quantitative Colorimetric Peptide Assay (Thermo Fisher 23275).  A total of six samples (3 open and 3 closed) plus four ‘pooled’ samples (created by combining equal volumes of each sample) were labeled with TMT10 reagents (Thermo Fisher 90406) at room temperature. Prior to quenching, the labeling efficiency was evaluated by LC-MS/MS analysis. After confirming >98% efficiency, samples were quenched with 50% hydroxylamine (Sigma-Aldrich 467804) to a final concentration of 0.4%. Labeled peptide samples were combined 1:1, cleaned using a peptide desalting spin column (Thermo Fisher 89852), and dried via vacuum centrifugation. The TMT-labeled sample was offline fractionated over a 90 minute run, into 96 fractions by high pH reverse-phase HPLC (Agilent 1260) using an Agilent Zorbax 300 Extend-C18 column (3.5-µm, 4.6 × 250 mm) with mobile phase A containing 4.5 mM ammonium formate (pH 10) (Sigma-Aldrich 70221) in 2% (vol/vol) LC-MS grade acetonitrile, and mobile phase B containing 4.5 mM ammonium formate (pH 10) in 90% (vol/vol) LC-MS grade acetonitrile (Sigma-Aldrich 271004-100), as previously described (Klomp et al. 2024; Mertins et al. 2018). The 96 resulting fractions were then concatenated in a non-continuous manner into 24 fractions and 5% of each were aliquoted, dried down via vacuum centrifugation and stored at -80 ºC until further analysis. The remaining 95% of each fraction was further concatenated into three fractions and dried down via vacuum centrifugation. For each fraction, phosphopeptides were enriched using the High Select Fe-NTA kit (Thermo Fisher A32992) per manufacturer protocol, then the Fe-NTA eluates were dried down via vacuum centrifugation and stored at -80 °C until further analysis. For each proteome sample, 205 µg of tryptic peptides were aliquoted and dried down.  All samples (24 proteome fractions; 3 phosphoproteome fractions, analyzed in duplicate) were analyzed by LC/MS/MS using an Ultimate 3000-Exploris480 (Thermo Fisher). Samples were injected onto an Ion Opticks Aurora C18 column (75 μm id × 15 cm, 1.6 μm particle size) and separated over a 70 (proteome) or 100 (phosphoproteome) minute method. The gradient for separation consisted of 5–42% mobile phase B at a 250 nl/minute flow rate, where mobile phase A was 0.1% formic acid in water and mobile phase B consisted of 0.1% formic acid in 80% acetonitrile The Exploris480 was operated in turboTMT mode with a cycle time of 3 seconds. Resolution for the precursor scan (m/z 375–1400) was set to 60,000 with an automatic gain control (AGC) target set to standard and a maximum injection time set to auto. MS2 scans (30,000 resolution) consisted of higher collision dissociate (HCD) set to 38; AGC target set to 300%; maximum injection time set to auto; isolation window of 0.7 Da; fixed first mass of 110 m/z."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Proteomic data analysis Raw data was processed by the Proteomics core using Proteome Discoverer (V3.1, Thermo Fisher) set to ‘reporter ion MS2’ with ‘10pex TMT’. Peak lists were searched against the A. thaliana database from Uniprot consisting of ~16,000 reviewed protein sequences, appended with a common contaminants database, using Sequest HT within Proteome Discoverer. Data were searched with up to two missed trypsin cleavage sites, fixed modifications: TMT6plex peptide N-terminus and Lys, carbamidomethylation Cys, dynamic modifications: N-terminal protein acetyl, oxidation Met. For phosphoproteome data, additional dynamic modification: phosphorylation Ser, Thr, Tyr. Precursor mass tolerance of 10 ppm and fragment mass tolerance of 0.02 Da (MS2). Peptide false discovery rate was set to 1%.  Reporter abundance was calculated based on intensity, and for MS2 data, co-isolation threshold was set to 30.   Data post-processing analysis was performed in R (v 4.4.1) using the MSstatsTMT and MSstatsPTM packages (Kohler et al. 2023; Huang et al. 2020). Global median normalization on the spectrum level data was performed. Spectrum level data was summarized to the protein level using Tukey’s median polish. To fulfill the requirements for imputation, there must be at least one nonmissing TMT channel for the same peptide spectrum match (PSM) in the run, and there must also be at least one nonmissing PSM from the same protein in the same TMT channel in that run. Statistical modeling and inference were performed using a linear mixed-effect model. The Benjamini-Hochberg (BH) method was used to adjust the p-values for multiple comparisons. The phosphoproteome abundance data has been adjusted (protein-adjusted phosphoproteome) to account for changes at the protein level using the MSstatsPTM package. Proportional Venn diagrams were created using the Deep Venn web tool from (Hulsen 2022)."],"omics_type":["Proteomics"],"labhead":["Marcela Rojas-Pierce"],"instrument_platform":[""],"submission_type":["PARTIAL"],"labhead_affiliation":["Department of Plant and Microbial Biology, North Carolina State University, Raleigh, NC 27514, USA"],"species":["Arabidopsis Thaliana (mouse-ear Cress)"],"publication":["10.1016/J.JPROT.2026.105681"],"submitter_mail":["scott_lyons@med.unc.edu"],"submitter_affiliation":["UNC Chapel Hill"],"submitter_country":["United States"],"additional_accession":[]},"is_claimable":false,"name":"Guard Cell-Enriched Phosphoproteome from open and closed stomata","description":"Control of the stomatal aperture is multifaceted, involving a complex interplay of environmental cues and intracellular signaling pathways. It is well established that changes in ion gradients drive water movement into and out of the guard cell, thereby altering cell volume and modulating the opening or closing of the stomatal pore. These rapid responses are often regulated by phosphorylation cascades to efficiently transmit environmental status and either reduce water loss or enhance carbon assimilation. Here, we investigated the regulation of stomatal opening and closing by generating a proteome and phosphoproteome of guard cell-enriched tissue. The guard cell-enriched tissue with closed stomata showed greater levels of phosphorylation of proteins related to endomembrane trafficking and vacuoles when compared to both whole leaf tissue with closed stomata and guard cell-enriched tissue with open stomata. These results support the hypothesis that phosphorylation of endomembrane proteins may contribute to the regulation of stomatal movements.","dates":{"publication":"2026-05-22","submission":"2025-10-29"},"accession":"PXD070005","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:1131","NEWT:35795","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:1334565","NEWT:625351","NEWT:258594","NCBITaxon:1280","NEWT:112503","NEWT:1129","NEWT:309807","NEWT:59753","NEWT:89184","NEWT:309800","NEWT:281395","NEWT:247480","NEWT:1211601","NEWT:876138","NEWT:44271","NEWT:193516","NEWT:2315688","NEWT:592321","NEWT:1073882","NEWT:6819","NEWT:475174","NEWT:1599","NEWT:428386","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:32264","NEWT:12215","NEWT:1590","NEWT:10034","NEWT:33114","NEWT:1596","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:294671","NEWT:376619","NEWT:1748418","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:3767","NEWT:1589","NEWT:135622","NEWT:4615","NEWT:672127","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:3760","NEWT:1584","NEWT:2086595","NEWT:36630","NEWT:1585","NEWT:383379","NEWT:381198","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","NEWT:317447","NEWT:4688","NEWT:3357","NEWT:7719","NEWT:29073","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:79329","NEWT:30069","NEWT:12637","NEWT:59729","NEWT:2164133","NEWT:295105","NEWT:108061","NEWT:60711","NEWT:2020713","NEWT:224308","NEWT:3347","NEWT:49928","NEWT:3349","NEWT:160621","NEWT:2502409","NEWT:212790","NEWT:110368","NEWT:1916073","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","NEWT:5516","NEWT:44688","NEWT:44689","NEWT:370038","NEWT:498211","NEWT:345076","NEWT:347256","NEWT:5518","NEWT:398007","NEWT:1527468","NEWT:498217","NEWT:498216","NEWT:11320","NEWT:246196","NEWT:246197","NEWT:145458","NEWT:1310173","NEWT:200795","NEWT:2579791","NEWT:44685","NEWT:161934","NEWT:1148","NEWT:5508","NEWT:3329","NEWT:419481","NEWT:5507","NEWT:260499","NEWT:410661","NEWT:329854","NEWT:1140","NCBITaxon:2157","NEWT:2066563","NEWT:2649329","NEWT:1143","NEWT:1287689","NEWT:1094343","NEWT:1462472","NEWT:1336795","NEWT:644042","NEWT:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NCBITaxon:37162","NEWT:270643","NEWT:3715","NEWT:2065263","NEWT:199225","NEWT:177437","NEWT:717966","NEWT:10891","NEWT:10418","NEWT:118698","NEWT:1616117","NEWT:118696","NEWT:34865","NEWT:52283","NEWT:28174","NEWT:284812","NEWT:8175","NEWT:43330","NEWT:1603293","NEWT:44664","NEWT:43346","NEWT:3702","NEWT:1245466","NEWT:3704","NEWT:244366","NEWT:1246791","NEWT:176597","NEWT:118694","NEWT:2850","NEWT:118691","NEWT:34871","NEWT:9006","NEWT:33548","NEWT:52299","NEWT:8165","NEWT:96794","NEWT:10886","NEWT:3708","NEWT:332648","NEWT:44670","NEWT:926571","NEWT:536231","NEWT:376219","NEWT:219813","NEWT:1510","NEWT:1955249","NEWT:460519","NEWT:1515","NEWT:572307","NEWT:1432138","NEWT:2714896","NEWT:1424507","NEWT:1194599","NEWT:272844","NEWT:1348799","NEWT:1608994","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:1122981","NEWT:2853422","NEWT:1122984","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:45972","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:2836","NEWT:376686","NEWT:237610","NEWT:95486","EFO:0001352","NEWT:119562","NEWT:1883446","NEWT:31345","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:987059","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:1509","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1579","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:1922344","NEWT:108458","NEWT:5936","NEWT:85692","NEWT:321967","NEWT:320637","NEWT:1078283","NEWT:3750","NEWT:983964","NEWT:11706","NEWT:32644","NEWT:527796","NEWT:279010","NEWT:499175","NEWT:109779","NEWT:3745","NEWT:1715989","NCBITaxon:4751","NEWT:3747","NEWT:1116234","NEWT:415978","NEWT:235455","NEWT:1255228","NEWT:410289","NEWT:191701","NEWT:373153","NEWT:1640278","NEWT:9054","NEWT:472","NEWT:940825","NEWT:29459","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:41122","NEWT:5911","NEWT:1328300","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:11723","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166314","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:29488","NEWT:1871049","NEWT:215402","NEWT:1547","NEWT:1290454","NEWT:3726","NEWT:906914","NEWT:81231006","NEWT:30455","NEWT:28141","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:548","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:2126348","NEWT:5180","NEWT:256737","NEWT:299467","NEWT:9541","NEWT:51350","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:542","NEWT:2903","NEWT:185579","NEWT:872227","NEWT:13076","NEWT:2587410","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:2126337","NEWT:550","NEWT:253237","NEWT:10804","NEWT:33941","NEWT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