{"database":"Pride","file_versions":[{"headers":{"Content-Type":["application/json"]},"body":{"files":{"Csv":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067892/NPER1.csv","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067892/WGA.csv"],"Raw":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067892/eb11355_tc-1217b_QIP.raw","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067892/eb11353_tc-1217a_QIP.raw"],"Mzxml":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067892/eb11353_tc_1217a_QIP.mzXML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067892/eb11355_tc_1217b_QIP.mzXML"],"Mzid":["ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067892/eb11353_tc-1217a_QIP.mzIdentML","ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067892/eb11355_tc-1217b_QIP.mzIdentML"]},"type":"primary"},"statusCode":"OK","statusCodeValue":200}],"scores":null,"additional":{"labhead_mail":["maxence.nachury@ucsf.edu"],"submitter":["Chia-Hsiang Chang"],"technology_type":["Data-dependent acquisition","Mass Spectrometry"],"software":["Not available"],"submitter_keywords":["Brain","Mouse","Proteome","Cilia"],"full_dataset_link":["https://www.ebi.ac.uk/pride/archive/projects/PXD067892"],"tissue":["Brain","Neuron"],"sample_protocol":["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 for 6 hours with 1 µg 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 (>97%), 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.    Liquid chromatography and tandem mass spectrometry. Mass spectrometric data were collected on an Orbitrap Eclipse mass spectrometer coupled to a Proxeon NanoLC-1000 UHPLC (Thermo Fisher Scientific). The 100 µm capillary column was packed in-house with 35 cm of Accucore 150 resin (2.6 μm, 150Å; ThermoFisher Scientific). Data were acquired for 180 min per run. A FAIMS 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 – 60,000; scan range – 400-1600 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 – 36; isolation window – 0.5 Th; maximum ion injection time – 100 ms."],"repository":["Pride"],"modification":[""],"quantification_method":[""],"data_protocol":["Database searching included all entries from the mouse UniProt. 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 50-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) < 180 across all TMT channels and < 0.5 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 V. Nachury"],"instrument_platform":[""],"labhead_affiliation":["University of California, San Francisco"],"submission_type":["PARTIAL"],"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":["chiaoceanblue@gmail.com"],"submitter_affiliation":["UCSF"],"submitter_country":["United States"],"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 Unveils Specialized Domains for Extrasynaptic Signaling on Neuronal Cilia","description":"Neuronal cilia have emerged as signaling hubs, but their molecular composition and integration with synaptic communication remain unexplored. Using an engineered Arl13b-TurboID mouse model, we achieved robust cilia-specific biotinylation and proteomic profiling across diverse cell types. Comparative analyses revealed that brain and kidney cilia share only half of their proteome, with neuronal cilia uniquely enriched in synaptic proteins, adhesion molecules, and neurotransmitter receptors. Surprisingly, several signaling and adhesion molecules localize to neuronal cilia in discrete patterns maintained by active retrieval mechanisms. 16-fold expansion microscopy of mouse cortex revealed that the NMDA receptor is non-randomly positioned on ciliary membranes near glutamatergic synapses, suggesting that cilia eavesdrop on synaptic activity. These findings highlight the diversity and specialization of mammalian ciliary proteomes and indicates that nanoscale organization may endow neuronal cilia with extrasynaptic 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