ArticleNature communications2025
Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes in C. elegans.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- PKD2-like proteins targetProceedings of the National Academy of Sciences of the United States of America · 2026Article
- AbioRxiv : the preprint server for biology · 2026Article
- Superoxide dismutase impacts extracellular vesicle shedding and uptake.Free radical biology & medicine · 2026Article
- Proximity labeling strategies in Caenorhabditis elegans: a comprehensive review.Cell communication and signaling : CCS · 2026Review
- Insights into the zebrafish left-right organizer's centrosomes and cilia via volume electron microscopy.Biology open · 2026Article
- RAP-2-independent roles formicroPublication biology · 2026Article
- Integrating endogenous TurboID and data-independent acquisition mass spectrometry for in vivo proximity labeling.The EMBO journal · 2026Article
- Advances in ciliary proteomics - towards cracking the hidden proteome code of cilia.Journal of cell science · 2025Review
- C. elegans: An elegant experimental system for the study of cilia biology.Seminars in cell & developmental biology · 2025Review
- Functionally Essential and Structurally Diverse: Insights into the zebrafish Left-Right Organizer's Cilia via Optogenetic IFT88 Perturbation and Volume Electron Microscopy.bioRxiv : the preprint server for biology · 2025Article
- Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes in C. elegans.Nature communications · 2025Article
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7 authors.
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Abstract
Therapeutic use of tiny extracellular vesicles (EVs) requires understanding cargo loading mechanisms. Here, we use a modular proximity labeling approach to identify the cargo of ciliary EVs associated with the transient receptor potential channel polycystin-2 PKD-2 of C. elegans. Polycystins are conserved ciliary proteins and cargo of EVs; dysfunction causes polycystic kidney disease in humans and mating deficits in C. elegans. We discover that polycystins localize with specific cargo on ciliary EVs: polycystin-associated channel-like protein PACL-1, dorsal and ventral polycystin-associated membrane C-type lectins PAMLs, and conserved tumor necrosis factor receptor-associated factor (TRAF) TRF-1 and TRF-2. Loading of these components to EVs relies on polycystin-1 LOV-1. Our modular EV-TurboID approach can be applied in both cell- and tissue-specific manners to define the composition of distinct EV subtypes, addressing a major challenge of the EV field.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.