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<p>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 <i>C. elegans</i>. Polycystins are conserved ciliary proteins and cargo of EVs; dysfunction causes polycystic kidney disease in humans and mating deficits in <i>C. elegans</i>. We discover that polycystins localize with specific cargo on ciliary EVs: <Emphasis Type="Underline">p</Emphasis>olycystin-<Emphasis Type="Underline">a</Emphasis>ssociated <Emphasis Type="Underline">c</Emphasis>hannel-<Emphasis Type="Underline">l</Emphasis>ike protein PACL-1, dorsal and ventral <Emphasis Type="Underline">p</Emphasis>olycystin-<Emphasis Type="Underline">a</Emphasis>ssociated <Emphasis Type="Underline">m</Emphasis>embrane C-type <Emphasis Type="Underline">l</Emphasis>ectins PAMLs, and conserved <Emphasis Type="Underline">t</Emphasis>umor necrosis factor&#xa0;<Emphasis Type="Underline">r</Emphasis>eceptor-<Emphasis Type="Underline">a</Emphasis>ssociated <Emphasis Type="Underline">f</Emphasis>actor (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.</p>

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Polycystins recruit cargo to distinct ciliary extracellular vesicle subtypes in C. elegans

  • 期刊论文

  • 出版模式：

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  • 发表日期：

    2025年4月3日

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  • Inna A. Nikonorova,
  • Elizabeth desRanleau,
  • Katherine C. Jacobs,
  • Josh Saul,
  • Jonathon D. Walsh,
  • Juan Wang,
  • Maureen M. Barr

摘要

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.