ArticleNature structural & molecular biology2026
The filamentous ultrastructure of the PopZ condensate is required for its cellular function.
Article in Nature structural & molecular biology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 4 papers.
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4 citing papers in PubMed.
- Probing biomolecular condensates with a minimally perturbative experimental readout framework.The Biochemical journal · 2026Review
- A tunable aqueous architecture modulates functional output in biomolecular condensates.bioRxiv : the preprint server for biology · 2026Article
- Plant NLRs are getting into higher-order architectures.The Plant journal : for cell and molecular biology · 2026Review
- Nanometer condensate organization in live cells derived from partitioning measurements.bioRxiv : the preprint server for biology · 2025Article
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Abstract
Biomolecular condensates have key roles in regulating cellular processes. Yet, the relationship between atomic features and condensate function remains poorly understood. We studied this relationship using the polar organizing protein Z (PopZ). Here, we revealed hierarchical assembly of PopZ into a filamentous condensate by integrating cryo-electron tomography, biochemistry, single-molecule techniques and molecular dynamics simulations. The PopZ helical domain drives filamentation and condensation, while the disordered region inhibits them. Phase-dependent conformational changes prevent interfilament contacts in the dilute phase and expose client-binding sites in the dense phase. Perturbing filament formation in vitro alters the dynamics of scaffold and client proteins and the condensate's wetting behavior. In cells, perturbing either filament formation or the ability of filaments to condense impairs PopZ function and leads to growth phenotypes. These findings establish a multiscale framework linking molecular interactions and condensate ultrastructure to cellular function.
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