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TitleStructural insights into SSNA1 self-assembly and its microtubule binding for centriole maintenance.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 7512, Year 2025
Publish dateAug 13, 2025
AuthorsLorenzo Agostini / Jason A Pfister / Nirakar Basnet / Jienyu Ding / Rui Zhang / Christian Biertümpfel / Kevin F O'Connell / Naoko Mizuno /
PubMed AbstractSSNA1 is a fibrillar protein involved in dynamic microtubule remodeling, including nucleation, co-polymerization, and microtubule branching. The underlying molecular mechanism has remained unclear ...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.
External linksNat Commun / PubMed:40804232 / PubMed Central
MethodsEM (helical sym.)
Resolution4.55 Å
Structure data

EMDB-47147, PDB-9dsm:
Cryo-EM structure of SSNA-1(R18E/R20E/Q98E) filaments
Method: EM (helical sym.) / Resolution: 4.55 Å

Source
  • caenorhabditis elegans (invertebrata)
KeywordsCELL CYCLE / SSNA1 / DIP13 / NA14 / microtubules / centriole / centrosome / mitotic spindle / cytoskeleton / coiled-coil

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