Structural insights into SSNA1 self-assembly and its microtubule binding for centriole maintenance

Lorenzo Agostini, Jason A. Pfister, Nirakar Basnet, Jienyu Ding, Rui Zhang, Christian Biertümpfel (), Kevin F. O’Connell () and Naoko Mizuno ()
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Lorenzo Agostini: 50 South Dr.
Jason A. Pfister: 8 Center Dr.
Nirakar Basnet: 50 South Dr.
Jienyu Ding: 50 South Dr.
Rui Zhang: School of Medicine
Christian Biertümpfel: 50 South Dr.
Kevin F. O’Connell: 8 Center Dr.
Naoko Mizuno: 50 South Dr.

Nature Communications, 2025, vol. 16, issue 1, 1-13

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-62696-9

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