PXD067626

PXD067626 is an original dataset announced via ProteomeXchange.

Title	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.
HostingRepository	PRIDE
AnnounceDate	2026-06-08
AnnouncementXML	Submission_2026-06-08_01:47:07.566.xml
DigitalObjectIdentifier	https://doi.org/10.6019/PXD067626
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Marian Kalocsay
SpeciesList	scientific name: Mus musculus (Mouse); NCBI TaxID: NEWT:10090;
ModificationList	No PTMs are included in the dataset
Instrument	Orbitrap Exploris 480; Orbitrap Ascend

Revision	Datetime	Status	ChangeLog Entry
0	2025-08-22 18:23:33	ID requested
⏵ 1	2026-06-08 01:47:08	announced

10.6019/PXD067626;

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, 12(23):eaed5548(2026) [pubmed]

10.1126/sciadv.aed5548;

submitter keyword: expansion microscopy,neuronal cilia, proximity proteomics, cilia-synapse interaction, synaptic signaling

Maxence Nachury
contact affiliation	Professor, Ophtalmology, School of Medicine, University of California, Sam Fancisco (UCSF)
contact email	Maxence.Nachury@ucsf.edu
lab head
Marian Kalocsay
contact affiliation	The University of Texas MD Anderson Cancer Center Department of Experimental Radiation Oncology
contact email	mkalocsay@mdanderson.org
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2026/06/PXD067626

PRIDE project URI

• PRIDE
  1. PXD067626
     1. Label: PRIDE project
     2. Name: In situ Proteomics of Brain Cilia Unveils Molecular Mechanisms of Cilia-Synapse Interactions