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Kalocsay"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":["Not available"],"submitter_keywords":["Synaptic signaling","Neuronal cilia","Expansion microscopy","Cilia-synapse interaction","Proximity proteomics"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067626"],"tissue":["Brain","Ciliated Cell"],"sample_protocol":["Dry beads were processed for TMT-MS3 as previously described (Shinde et al., 2023) by the Thermo Fisher Scientific Center for Multiplexed Proteomics (TCMP) at Harvard Medical School for the total extract experiment ➊ and the membrane protein experiment ➌ or by the Kalocsay lab for total extract experiment (Ascend instrument) ➋. Data of supplementary figures S4E-H were recorded on an OE480 instrument. In brief, samples were processed with the following steps: On Bead Digestion and Labeling: Protein-coated beads were washed three times with PBS. The beads were suspended in 200 mM EPPS pH 8.5 and digested over night with 1µg trypsin. Acetonitrile was added to each sample to achieve a final concentration of ~33%. Each sample was labelled with ~62.5 µg of TMTPro reagents (ThermoFisher Scientific). Following confirmation of satisfactory labelling (>95%), excess TMT was quenched by addition of hydroxylamine to a final concentration of 0.3%. The full volume from each sample was pooled and acetonitrile was removed by vacuum centrifugation. The samples were acidified with formic acid and desalted by StageTip eluted into autosampler inserts (Thermo Scientific), dried in a speedvac and reconstituted with 5% Acetonitrile, 5% formic acid for LC-MS/MS analysis. Samples (Kalocsay lab) were subjected to alkaline reversed phase chromatography using the high-pH reversed phase peptide fractionation kit (Thermo Scientific #84868) and combined into 6 fractions or 12 fractions. Liquid chromatography and tandem mass spectrometry: Mass spectrometric data were collected on an Orbitrap Exploris 480 (Kalocsay lab) or Ascend (Kalocsay lab) mass spectrometer coupled to a VanquishNeo UHPLC (Thermo Fisher Scientific). The 75 µm capillary column was packed in-house with 35 cm of Accucore 150 resin (2.6 μm, 150Å; ThermoFisher Scientific). Data was acquired for 60 min (OE480, 6 fractions) or 90 min (Ascend, 12 fractions) per run. A FAIMS ProDuo2 device was enabled during data collection and compensation voltages were set at -40V, -60V, and -80V [PMID: 30672687]. MS1 scans were collected in the Orbitrap (resolution – 120,000; scan range – 350-1400 Th; automatic gain control (AGC) – 4x105; maximum ion injection time – automatic). MS2 scans were collected in the Orbitrap following higher-energy collision dissociation (HCD; resolution – 50,000; AGC – 1.25x105; normalized collision energy – 33; isolation window – 0.7 Th; maximum ion injection time – 96 ms (OE480) or 400 ms (Ascend)."],"repository":["Pride"],"quantification_method":[""],"modification":[""],"data_protocol":["Mass Spectrometry Data Analysis: Database searching included all entries from the mouse UniProt Database. The database was concatenated with one composed of all protein sequences for that database in the reversed order [PMID: 17327847]. Raw files were converted to mzXML, and monoisotopic peaks were re-assigned using Monocle [PMID: 33190505].  Searches were performed with Comet [PMID: 23148064] using a 20-ppm precursor ion tolerance and fragment bin tolerance of 0.02.  TMTpro labels on lysine residues and peptide N-termini (+304.207 Da), as well as carbamidomethylation of cysteine residues (+57.021 Da) were set as static modifications, while oxidation of methionine residues (+15.995 Da) was set as a variable modification. Peptide-spectrum matches (PSMs) were adjusted to a 1% false discovery rate (FDR) using a linear discriminant after which proteins were assembled further to a final protein-level FDR of 1% analysis [PMID: 21183079].  TMT reporter ion intensities were measured using a 0.003 Da window around the theoretical m/z for each reporter ion. Proteins were quantified by summing reporter ion counts across all matching PSMs. More specifically, reporter ion intensities were adjusted to correct for the isotopic impurities of the different TMTpro reagents according to manufacturer specifications. Peptides were filtered to exclude those with a summed signal-to-noise (SN) < 200 across all TMT channels and < 0.7 precursor isolation specificity.  The signal-to-noise (S/N) measurements of peptides assigned to each protein were summed (for a given protein)."],"omics_type":["Proteomics"],"labhead":["Maxence Nachury"],"instrument_platform":[""],"labhead_affiliation":["Professor, Ophtalmology, School of Medicine, University of California, Sam Fancisco (UCSF)"],"submission_type":["COMPLETE"],"species":["Mus Musculus (mouse)"],"publication":["42234764 Chang CH, Trinh VN, Novak SW, Lokesh NR, Montecinos CK, Boassa D, Pownall ME, Kalocsay M, Nachury MV. In situ proteomics unveils specialized domains for extrasynaptic signaling on neuronal cilia. Sci Adv. 2026 12(23):eaed5548 10.1126/sciadv.aed5548"],"submitter_mail":["mkalocsay@mdanderson.org"],"submitter_affiliation":["The University of Texas MD Anderson Cancer Center\nDepartment of Experimental Radiation Oncology"],"submitter_country":["United States"],"doi":["10.6019/PXD067626"],"pubmed_abstract":["Neuronal cilia have emerged as crucial signaling hubs, yet their molecular composition and integration with synaptic communication remain poorly understood. Using a newly developed <i>Arl13b-TurboID</i> mouse model, we achieved robust cilia-specific biotinylation and proteomic profiling across diverse tissues and cell types. Comparative proteomics revealed notable tissue-specific specialization, with neuronal cilia uniquely enriched in synaptic proteins, adhesion molecules, and neurotransmitter receptors. Unexpectedly, several signaling and adhesion molecules localize to neuronal cilia in discrete nanodomains maintained by active retrieval mechanisms. In the mouse cortex, expansion microscopy revealed that the NMDA receptor subunit GluN1 is organized in nanodomains on neuronal ciliary membranes, which are precisely positioned to sample neurotransmitter efflux from neighboring glutamatergic synapses. These findings establish neuronal cilia as specialized extrasynaptic signaling platforms, with nanoscale organization enabling them to integrate local synaptic cues and modulate neuronal connectivity."],"pubmed_title":["In situ proteomics unveils specialized domains for extrasynaptic signaling on neuronal cilia."],"pubmed_authors":["Chang Chia-Hsiang CH, Trinh Van Ngu VN, Novak Sammy Weiser SW, Lokesh Nidhi Rani NR, Montecinos Catalina Kretschmar CK, Boassa Daniela D, Pownall Mark E ME, Kalocsay Marian M, Nachury Maxence V MV"],"additional_accession":[]},"is_claimable":false,"name":"In situ Proteomics of Brain Cilia Unveils Molecular Mechanisms of Cilia-Synapse Interactions","description":"Neuronal cilia have emerged as pivotal signaling hubs; yet the ciliary molecules that organize signaling modalities and communication with neighboring synapses remain elusive. To map the brain cilia proteome, we engineered an Arl13b-TurboID mouse that enabled robust cilia-specific biotinylation in all cell types. Comparative quantitative proteomics revealed that neuronal and kidney cilia share less than half of their proteome. The brain cilia proteome encompasses synaptic proteins, transporters, adhesion molecules, and neurotransmitter receptors. Surprisingly, several signaling and adhesion molecules localize on neuronal cilia in discrete patterns, which are actively established. Mapping the NMDA receptor GluN1 at 25 nm resolution in the mouse cortex revealed a close, non-random association between ciliary GluN1 molecules and neighboring glutamatergic synapses. Cilia may thus eavesdrop on synaptic communication by re-deploying parts of the synaptic apparatus. Our study highlights the diversity and specialization of mammalian ciliary proteomes and indicates that nanoscopic organization may endow neuronal cilia with extrasynaptic functions.","dates":{"publication":"2026-06-08","submission":"2025-08-23"},"accession":"PXD067626","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:156587","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: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: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: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:51329","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:305959","NEWT:102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