ArticleNature communications2025
Structural insights into SSNA1 self-assembly and its microtubule binding for centriole maintenance.
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 5 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
5 citing papers in PubMed.
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- The luminal ring protein C2CD3 acts as a radial in-to-out organizer of the distal centriole and appendages.PLoS biology · 2025Article
- C. elegans SAS-1 ensures centriole integrity and ciliary function, and operates with SSNA-1.PLoS genetics · 2025Article
- C. elegans SSNA-1 is required for the structural integrity of centrioles and bipolar spindle assembly.Nature communications · 2025Article
- ThebioRxiv : the preprint server for biology · 2024Article
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8 authors.
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Abstract
SSNA1 is a fibrillar protein involved in dynamic microtubule remodeling, including nucleation, co-polymerization, and microtubule branching. The underlying molecular mechanism has remained unclear due to a lack of structural information. Here, we determine the cryo-EM structure of C.elegans SSNA-1 at 4.55-Å resolution and evaluate its role in embryonic development. We find that SSNA-1 forms an anti-parallel coiled-coil, with self-assembly facilitated by an overhang of 16 C-terminal residues that form a triple-stranded helical junction. The microtubule-binding region is within the triple-stranded junction, suggesting that self-assembly of SSNA-1 creates hubs for effective microtubule interaction. Genetical analysis elucidates that SSNA-1 deletion significantly reduces embryonic viability, and causes multipolar spindles during cell division. Interestingly, impairing SSNA-1 self-assembly has a comparable effect on embryonic viability as the knockout strain. Our study provides molecular insights into SSNA-1's self-assembly and its role in microtubule binding and cell division regulation through centriole stability.
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