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Lam"],"technology_type":["Data-dependent acquisition","Mass Spectrometry","Bottom-up proteomics"],"software":[""],"submitter_keywords":["Learned helplessness","Mpfc","Stress models","Proteomics","Acetylcholine","Muscarinic receptors","Major depressive disorder"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD073765"],"tissue":["Brain"],"sample_protocol":["Five min following the last trial of active avoidance testing, mice were euthanized and the mPFC was dissected and homogenized in SynPER Synaptic Protein Extraction Reagent with protease and phosphatase inhibitors and then spun at 12,000 x g for 10 min at 4° C. The supernatant was collected and spun at 15,000 x g for 20 min at 4° C. The pellet from this spin contained the synaptosomal fraction, which was resuspended in SynPER without inhibitors, washed, and resuspended in SynPER without inhibitors. Protein concentration was determined via BCA (ThermoFisher), samples were diluted to 15 µg and additional sample preparation was carried out by the Discovery Proteomics Core of the Yale/NIDA Neuroproteomics Center for bottom-up Label-Free Quantification (LFQ) proteomics.   Synaptosomes were dried and resuspended in 50 µL solubilization buffer (8 M urea in 0.4 M ammonium bicarbonate) and sonicated in a water bath for 1 h at 39° C. Disulfides in proteins were reduced with 5 µL of 45 mM dithiothreitol (DTT) and incubated at 37° C for 30 min then allowed to cool to room temperature. Free cysteines were then alkylated with 5 µL of 100 mM iodoacetamide (IAN) and incubated in the dark at room temperature for 30 min. After diluting with water (78 µL of H2O added to mixture) to bring the urea concentration to 2 M. 2 µL of a 0.5 µg/µL stock sequencing-grade Lys C was added and allowed to digest overnight at 37° C. Then 2 µL of a 0.5 µg/µL stock sequencing-grade trypsin (Promega, Madison, WI, USA) was added and incubated at 37° C for an additional 6 hr. The digestions were quenched by acidifying with 7.1 uL of 20% trifluoro acetic acid, then stored at -20° C until further analysis. Digested samples were then desalted using a C18 spin column (The Nest Group, Inc., Southborough, MA, USA) and dried in a rotary evaporator. Dried pellets were resuspended in 70 mM L-glutamic acid and phospho-enriched with Glygen Top Tips 1-10 µL TiO2 column (Glygen Corp.) in modified buffer (21). The flowthrough fractions and enriched fractions were dried in a SpeedVac without heat. Dried samples were resuspended in 0.2% trifluoroacetic acid (TFA) and 2% acetonitrile (ACN) in water for LC MS/MS analysis. Nanodrop readings were taken to ensure equal total peptides were injected/analyzed for each sample. Prior to injection onto the Waters M-Class UPLC (Waters Corporation, Milford, MA, USA) coupled to the Q-Exactive HFX mass spectrometer (ThermoFisher Scientific, San Jose, CA, USA), Pierce Retention Time Calibration Mix (RTCalMix) standards were spiked into all samples. After injection, samples were loaded onto a trapping column (nanoEase M/Z Symmetry C18 Trap column, 180 µm × 20 mm) at a flow rate of 10 µL/min and separated on an RP C18 column (nanoEase M/Z column Peptide BEH C18, 75 µm × 250 mm). The composition of mobile phases A and B were 0.1% formic acid in water and 0.1% formic acid in ACN, respectively. Peptides were separated and eluted with a gradient extending from 6% to 25% mobile phase B over 173 min, then to 40% over 20 min and then to 90% over another 5 min at a flow rate of 300 nL/min and a column temperature of 37° C. Column regeneration and up to three blank injections were carried out between all sample injections. Data were acquired with the mass spectrometer operating in a data-dependent mode (DDA). The full scan was performed in the range of 350-1,500 m/z with “Use Quadrupole Isolation” enabled at an Orbitrap resolution of 120,000 at 200 m/z and automatic gain control (AGC) target value of 3 × 106 and fragment ions from each peptide MS2 were generated in the C-trap with higher-energy collision dissociation (HCD) at a normalized collision energy of 30% and detected in the Orbitrap at a resolution of 30,000. Full scan was followed by MS2 events of the most intense ions above an intensity threshold of 1 × 104. The ions were iteratively isolated with a 1.4 Th window, injected with a maximum injection time of 50 milliseconds, AGC target of 1 × 105, a dynamic exclusion length of 30 seconds, and fragmented with higher-energy collisional dissociation (HCD). Two blanks (1st 100 % ACN, 2nd Buffer A) followed each injection to ensure there was no sample carry over."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Protein expression exchanges data from Progenesis QI were prefiltered to exclude proteins with fewer than 2 unique identified peptides and Mascot score more than 30.  For phosphorylation site (phosphosite) quantitative comparisons among the different conditions, we utilized the peptide level identification and abundance results from Progenesis QI along with a custom Python script to retrieve and map the phosphosites onto known protein sequence from UniProtKB/Swiss-Prot database (Release 2025_04 https://www.uniprot.org/,).  Only proteins (from protein level analysis) and phosphosites (from peptide level analyses) detected in all groups were used for differential expression analysis. Both protein and phosphopeptide abundances were log2-transformed and median normalization was applied using RStudio version 2025.09.1+401 (Posit Software, PBC). UpSet plots were created using custom written R code. Multigroup comparison was done by ANOVA with FDR p < 0.1 to identify clusters of differentially abundant proteins (DAP) and summed localized phosphosite abundances (e.g. different phosphopeptides abundanes were summed if they share the same phosphosite ID mapped according to UniProtKB/Swiss-Prot database, see above) across all groups. Pairwise comparison was done by unpaired two-tailed t-test p<0.05, False Discovery Rate (FDR p<0.1). Differential expression of phosphosite was subsequently assessed by unpaired t-test. A threshold of a 0.5 log2-fold change combined with FDR p < 0.1 was applied to define significantly differentially expressed phosphosites. Qlucore Omics Explorer version 3.9 (Qlucore, Lund, Sweden) was used for data visualization including principal component analysis (PCA), and global proteomics change across the groups by volcano plot. Overrepresentation analyses (Fisher’s exact test FDR p < 0.05) of differentially abundant proteins and phosphoproteins were carried out using Ingenuity Pathway Analysis (Qiagen, version 145030503) to determine enriched pathways, and biological functions. Kinase activity was predicted using the Kinase-Substrate Enrichment Analysis (KSEA) algorithm in the KSEA app using RStudio version 2025.09.1+401 (Posit Software, PBC) selecting the PhosphoSitePlus database for curated annotations, p-value cutoff 0.05, and substrate count cutoff 5."],"omics_type":["Proteomics"],"labhead":["TuKiet Lam"],"instrument_platform":[""],"labhead_affiliation":["Keck MS & Proteomics Resource Yale School of Medicine"],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"submitter_mail":["tukiet.lam@yale.edu"],"publication":["41980822 Abdulla ZI, Garcia-Milian R, Giahyue E, Fertuzinhos S, Collin F, Wang W, Lam TT, Nairn AC, Picciotto MR. mPFC Synaptosome Proteomics Reveals Novel Pathways and Muscarinic Receptor Changes in a Learned Helplessness Mouse Model. eNeuro. 2026:ENEURO.0030-26.2026 10.1523/eneuro.0030-26.2026"],"submitter_affiliation":["Yale University"],"submitter_country":["United States"],"pubmed_abstract":["Stressful events are a leading factor in the development of depression. The medial prefrontal cortex (mPFC) is strongly associated with depression etiology and exposure to uncontrollable stressors results in synaptic dysfunction and loss. Learned helplessness is a behavioral paradigm that measures effects of repeated exposure to uncontrollable, inescapable stress on later responses to escapable stress. We therefore performed a proteomic analysis of mPFC synaptosomes in a mouse learned helplessness model to identify molecular changes that could contribute to functional consequences of inescapable stress. Male and female mice were evaluated at baseline and following exposure to escapable or inescapable stress followed by an active avoidance test. Label-free mass spectrometry followed by pathway and protein-protein interaction network analyses identified alterations in signaling pathways involved in energy metabolism, neurotransmitter signaling, and protein shuttling. Furthermore, phosphoproteomics revealed alterations related to synaptic function, neurotransmitter signaling and protein internalization, as well as changes in activity of kinases previously identified as mediators of antidepressant efficacy (GSK3B) and receptor internalization (ADRBK1). We more deeply examined alterations in the acetylcholine receptor signaling pathway and identified muscarinic receptor proteins (Chrm1, Chrm2, Chrm4) and key proteins involved in their translocation to and from the membrane. These results identify substantial changes in the mPFC proteome following exposure to inescapable stressors. In addition, mPFC muscarinic cholinergic signaling is well placed to mediate responses to an inescapable stressor. This proteomic study will be useful in guiding studies of human mPFC relevant to depression. Data are available via ProteomeXchange with identifier PXD073765."],"pubmed_title":["mPFC Synaptosome Proteomics Reveals Novel Pathways and Muscarinic Receptor Changes in a Learned Helplessness Mouse Model."],"pubmed_authors":["Abdulla Zuhair I ZI, Garcia-Milian Rolando R, Giahyue Ernestine E, Fertuzinhos Sofia S, Collin Florine F, Wang Weiwei W, Lam TuKiet T TT, Nairn Angus C AC, Picciotto Marina R MR"],"additional_accession":[]},"is_claimable":false,"name":"mPFC Synaptosome Proteomics Reveals Novel Pathways and Muscarinic Receptor Changes in a Learned Helplessness Mouse Model","description":"Stressful events are a leading factor in development of depression. The medial prefrontal cortex (mPFC) is strongly associated with depression etiology and exposure to uncontrollable stressors results in synaptic dysfunction and loss. Learned helplessness is a behavioral paradigm that measures effects of repeated exposure to uncontrollable, inescapable stress on later responses to escapable stress. We therefore performed a proteomic analysis of mPFC synaptosomes in a mouse learned helplessness model to identify molecular changes that could contribute to functional consequences of inescapable stress. Male and female mice were evaluated at baseline and following exposure to escapable or inescapable stress followed by an active avoidance test. Label-free mass spectrometry followed by pathway and protein-protein interaction network analyses identified alterations in signaling pathways involved in energy metabolism, neurotransmitter signaling, and protein shuttling. Furthermore, phosphoproteomics revealed alterations related to synaptic function, neurotransmitter signaling and protein internalization, as well as changes in activity of kinases previously identified as mediators of antidepressant efficacy (GSK3B) and receptor internalization (ADRBK1). We more deeply examined alterations in the Acetylcholine Receptor Signaling Pathway, and identified muscarinic receptor proteins (Chrm1, Chrm2, Chrm4) and key proteins involved in their translocation to and from the membrane. These results identify substantial changes in the mPFC proteome following exposure to inescapable stressors. In addition, mPFC muscarinic cholinergic signaling is well placed to mediate responses to an inescapable stressor. This proteomic study will be useful in guiding studies of human mPFC relevant to depression","dates":{"publication":"2026-04-20","submission":"2026-01-29"},"accession":"PXD073765","cross_references":{"TAXONOMY":["NEWT:108018","NEWT:377960","NEWT:1131","NEWT:190486","NEWT:2737160","NEWT:2042546","NEWT:148942","NEWT:193528","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:10031","NEWT:82569","NEWT:661410","NEWT:488003","NEWT:224326","NEWT:376619","NEWT:3765","NEWT:2433","NEWT:1190602","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:641809","NEWT:44250","NEWT:77151","NEWT:317447","NEWT:698761","NEWT:5530","NEWT:868565","NEWT:135674","NEWT:1562698","NEWT:11308","NEWT:12637","NEWT:2164133","NEWT:1180","NEWT:2767846","NEWT:1343074","NEWT:314344","NEWT:108061","NEWT:143292","NEWT:2767842","NEWT:314345","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: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:32201","NEWT:34869","NEWT:226126","NEWT:1616117","NEWT:34865","NEWT:550537","NEWT:284812","NEWT:284811","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:1195466","NEWT:2483192","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: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:427924","NEWT:2003758","NEWT:29486","NEWT:63366","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:29471","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:480020","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:206411","NEWT:80869","NEWT:214053","NEWT:80863","NEWT:665890","NEWT:52639","NEWT:5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