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Chen"],"technology_type":["Mass Spectrometry","Data-independent acquisition"],"software":[""],"submitter_keywords":["Lrrk2","Apex2","Proteome analysis"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD065003"],"tissue":["Brain"],"sample_protocol":["This analysis was performed in Biognosys AG (Schlieren, Switzerland). Samples (beads with proteins attached via streptavidin pulldown)  were solubilized and digested overnight with sequencing grade trypsin (Promega) in a urea-containing denaturation buffer. Each sample is the eluted proteins from one mouse: 4-8 mice/genotype, treatment combination as shown in Supplementary Figure 3except Cre- control mice n=2 mice/condition. Beads were collected on a magnetic rack, supernatant was transferred to a new tube and used for the clean-up. Purification for mass spectrometry was carried out using Oasis HLB μElution Plate 30μm plate (WATERS) according to the manufacturer’s instructions. Peptides were dried down to complete dryness using a SpeedVac system and dissolved in LC solvent A (1 % acetonitrile in water with 0.1 % formic acid (FA)) containing Biognosys’ iRT-peptide mix for retention time calibration. Peptide concentrations in mass spectrometry ready samples were measured using the mBCA assay (Thermo Scientific Pierce). For DIA LC-MS/MS measurements, peptides were injected on an in-house packed reversed phase column on a Thermo Scientific EASY-nLC 1200 nano-liquid chromatography system connected to a Thermo Scientific Orbitrap Exploris 480 mass spectrometer equipped with a Nanospray Flex ion source and a FAIMS Pro ion mobility device (Thermo Scientific). LC solvents were A: water with 0.1 % FA; B: 80 % acetonitrile, 0.1 % FA in water. The nonlinear LC gradient was 1 – 50 % solvent B in 171 minutes followed by a column washing step in 90 % B for 7 minutes, and a final equilibration step of 1 % B for 0.5 column volumes at 64 °C with a flow rate set to a ramp between 450 to 271 nl/min (min 0: 450 nl/min, min 172: 271 nl/min, washing at 400 nl/min). The FAIMS-DIA method consisted per applied compensation voltage of one full range MS1 scan and 34 DIA segments as adopted from Bruderer et al. and & Tognetti et al."],"repository":["Pride"],"modification":[""],"quantification_method":["Not available"],"data_protocol":["The DIA mass spectrometric data were analyzed using Spectronaut software (Biognosys, version 19.0). The false discovery rate on peptide and protein level was set to 1 %. A mouse UniProt .fasta database (Mus musculus, 2024-07-01) was used for the search engine, allowing for 2 missed cleavages, carbamidomethylation of cysteine as fixed modification and up to 5 variable modifications (N-terminal acetylation, methionine oxidation, deamidation of asparagine or glutamine and phosphorylation at serine or threonine or tyrosine).   HRM mass spectrometric data were analyzed using Spectronaut software (Biognosys, version 19.0). The false discovery rate on peptide and protein level was set to 1 %, data was filtered using row-based extraction. The directDIA+ library generated in this project was used for the analysis. The HRM measurements analyzed with Spectronaut were normalized using global median normalization.   Proteins that were not enriched (enriched: q-value < 0.05, log2fc > 0) in Anxa1Cre; Lrrk2G2019S vehicle vs. non-transgenic ctrl were removed from the dataset of samples from SNc and striatum, respectively. The filtered dataset was used for further analysis. For testing of differential protein abundance, protein intensities for each protein were analyzed using a two-sample Student’s t-test. The following thresholds were applied for candidate identification: p-value < 0.05; absolute average log2 ratio > 0.58 (fold-change > 1.5). Distance in heat maps was calculated using the “manhattan” method, the clustering using “ward.D” for both axes. Principal component analysis was conducted in R using prcomp and a modified ggbiplot function for plotting. Functional analysis was performed using String-db (string-db.org, version 12.0).   Phospho-site summarization was carried out as described using a PTM localization probability cutoff of > 0.75 and linear model as aggregation type. For testing of differential phospho-site abundance, phosphosite intensities for each protein were analyzed using a two sample Student’s t test. The following thresholds were applied for candidate identification: p- value <0.05; absolute average log2 ratio > 0.58 (fold change > 1.5)"],"omics_type":["Proteomics"],"labhead":["Loukia Parisiadou"],"instrument_platform":[""],"labhead_affiliation":["Department of Pharmacology, Northwestern University, Chicago, IL, USA."],"submission_type":["PARTIAL"],"species":["Mus Musculus (mouse)"],"publication":["40909700 Chen C, He Q, Tombesi G, Napier E, Jaconelli M, Moreno-Ramos OA, Serio H, Naaldijk Y, Promes V, Schneeweis A, Quinn K, Nasios C, Greggio E, Kozorovitskiy Y, Arango D, Khan AR, Alessi DR, Dombeck DA, Hilfiker S, Awatramani R, Parisiadou L. Leucine-rich repeat kinase 2 impairs the release sites of Parkinson's disease vulnerable dopamine axons. bioRxiv. 2025:2025.08.28.672006 10.1101/2025.08.28.672006"],"submitter_mail":["chuyu.chen@northwestern.edu"],"submitter_affiliation":["Northwestern university"],"submitter_country":["United States"],"pubmed_abstract":["The end-stage pathology of Parkinson's disease (PD) involves the loss of dopamine-producing neurons in the substantia nigra pars compacta (SNc). However, synaptic deregulation of these neurons begins much earlier. Understanding the mechanisms behind synaptic deficits is crucial for early therapeutic intervention, yet these remain largely unknown. In the SNc, different dopamine neuron subtypes show varying susceptibility patterns to PD, complicating our understanding. This study uses intersectional genetic mouse models to uncover synaptic perturbations in vulnerable dopamine neurons, focusing on the LRRK2 kinase, a protein closely linked to PD. Through a combination of immunofluorescence and advanced proximity labeling methods, we found higher LRRK2 expression in the most vulnerable dopamine neuron subclusters. High-resolution imaging revealed that pathogenic LRRK2 disrupts release sites in vulnerable dopamine axons, leading to decreased in vivo evoked striatal dopamine release in mice with LRRK2 mutations. Proteomic and biochemical analyses indicate that mutant LRRK2 increases the phosphorylation of RAB3 proteins, reducing their interactions with RIM1/2 effector proteins and impacting their synaptic functions. Overall, this research highlights the cell-autonomous dysfunctions caused by mutant LRRK2 in the neurons that are primarily affected by the disease. It also provides a framework for therapeutic strategies for early nigrostriatal synaptic deficits in PD."],"pubmed_title":["Leucine-rich repeat kinase 2 impairs the release sites of Parkinson's disease vulnerable dopamine axons."],"pubmed_authors":["Chen Chuyu C, He Qianzi Q, Tombesi Giulia G, Napier Eve E, Jaconelli Matthew M, Moreno-Ramos Oscar Andrés OA, Serio Hannah H, Naaldijk Yahaira Y, Promes Vanessa V, Schneeweis Amanda A, Quinn Kaitlyn K, Nasios Christopher C, Greggio Elisa E, Kozorovitskiy Yevgenia Y, Arango Daniel D, Khan Amir R AR, Alessi Dario R DR, Dombeck Daniel A DA, Hilfiker Sabine S, Awatramani Rajeshwar R, Parisiadou Loukia L"],"additional_accession":[]},"is_claimable":false,"name":"The Parkinson’s disease kinase LRRK2 impairs release sites of vulnerable dopamine axons-APEX2 proteome analysis","description":"We and others previously reported that knock-in mice expressing the pathogenic hyperactive Lrrk2G2019S mutation, exhibit deficits in dopamine release within the striatum. To investigate the underlying molecular mechanisms, we conducted axonal proteome analysis of a subcluster within vulnerable Aldh1a1+ dopamine axons, defined by Annexin 1 (Anxa1+), confirmed subtle proteomic changes across comparisons","dates":{"publication":"2026-05-19","submission":"2025-06-13"},"accession":"PXD065003","cross_references":{"TAXONOMY":["NEWT:330879","NEWT:377960","NEWT:2042546","NEWT:259447","NEWT:295546","NCBITaxon:2719036","NEWT:625351","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:6819","NEWT:475174","NEWT:1117","NEWT:498257","NEWT:10036","NEWT:1590","NEWT:10034","NEWT:661410","NEWT:638632","NEWT:224326","NEWT:376619","NCBITaxon:79857","NEWT:1096976","NEWT:3765","NEWT:1589","NEWT:135622","NEWT:35786","NEWT:1580","NEWT:399784","NEWT:96731","NEWT:656064","NEWT:1582","NEWT:36630","NEWT:383379","NEWT:418106","NCBITaxon:12721","NEWT:10029","NEWT:913645","NEWT:641809","NEWT:1392488","NEWT:38815","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:110368","NEWT:1310161","NEWT:77133","NEWT:145481","NEWT:1310165","NEWT:29058","NCBITaxon:79824","NEWT:410658","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:150808","NEWT:1182590","NEWT:3712","NEWT:3711","NEWT:3714","NEWT:270643","NEWT:2065263","NEWT:177437","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:33548","NEWT:52299","NEWT:8165","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:1348799","NEWT:33995","NEWT:55784","NEWT:1303443","NEWT:9483","NEWT:485","NEWT:56636","NEWT:2499525","NEWT:2853422","NEWT:487","NEWT:1538553","NEWT:1679718","NEWT:480","NEWT:67767","NEWT:46835","NEWT:109757","NEWT:582580","NEWT:1185650","NEWT:216778","NEWT:1502","NEWT:128017","NEWT:376686","NEWT:237610","NEWT:95486","NEWT:1883446","NEWT:1233435","NEWT:118223","NEWT:11757","NEWT:109760","NEWT:29031","NEWT:317047","NEWT:491","NEWT:460523","NEWT:45954","NEWT:235443","NEWT:1757312","NEWT:85694","NEWT:109786","NEWT:108458","NEWT:5936","NEWT:320637","NEWT:1078283","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:1640278","NEWT:472","NEWT:940825","NEWT:529507","NEWT:1071661","NEWT:28128","NEWT:470","NEWT:5911","NEWT:748693","NCBITaxon:50557","NEWT:39251","NEWT:29491","NEWT:101841","NEWT:446","NEWT:153481","NEWT:2014887","NEWT:33952","NEWT:445","NEWT:153009","NEWT:261756","NEWT:166313","NEWT:63366","NEWT:63367","NEWT:215402","NEWT:1547","NEWT:906914","NEWT:9031","NEWT:27292","NEWT:1050722","NEWT:3728","NEWT:108931","NEWT:1293497","NEWT:1055524","NEWT:150475","NEWT:267872","NEWT:381666","NEWT:172269","NEWT:9534","NEWT:5180","NEWT:256737","NEWT:9541","NEWT:8694","NEWT:33936","NEWT:8692","NEWT:2903","NEWT:185579","NEWT:13076","NEWT:207340","NEWT:1006581","NEWT:8673","NEWT:33940","NEWT:550","NEWT:554","NEWT:451516","NEWT:552","NEWT:1325291","NEWT:36185","NEWT:1054211","NEWT:1225786","NEWT:771870","NEWT:51338","NEWT:575412","NEWT:28112","NEWT:6493","NEWT:10832","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:9983","NEWT:8655","NEWT:5147","NEWT:28108","NEWT:28104","NEWT:407821","NEWT:568703","NCBITaxon:2","NEWT:568708","NEWT:1613","NEWT:986","NEWT:52641","NEWT:28532","NEWT:353152","NEWT:298176","NEWT:353153","NEWT:227377","NEWT:1774284","NEWT:40674","NEWT:1194669","NEWT:443906","NEWT:519","NEWT:2510939","NEWT:7394","NEWT:6063","NEWT:1328388","NEWT:105487","NEWT:1548728","NEWT:667127","NEWT:9557","NEWT:377586","NEWT:300641","NEWT:39655","NEWT:9554","NEWT:38323","NEWT:475932","NEWT:256318","NEWT:206411","NCBITaxon:6191","NEWT:229533","NEWT:214053","NEWT:28550","NEWT:80863","NEWT:90675","NEWT:52639","NEWT:52638","NEWT:57075","NEWT:1666905","NEWT:8697","NEWT:8695","NEWT:884204","NEWT:1045775","NEWT:1123869","NEWT:9544","NEWT:9545","NEWT:979","NEWT:7370","NEWT:83906","NEWT:99488","NEWT:1134506","NEWT:255470","NEWT:38783","NEWT:6426","NEWT:33090","NEWT:9935","NEWT:287889","NEWT:3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