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

Author

Listed:
  • Lorenzo Agostini

    (50 South Dr.)

  • Jason A. Pfister

    (8 Center Dr.)

  • Nirakar Basnet

    (50 South Dr.
    Institute for Protein Innovation)

  • 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.
    50 South Dr.)

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.

Suggested Citation

  • Lorenzo Agostini & Jason A. Pfister & Nirakar Basnet & Jienyu Ding & Rui Zhang & Christian Biertümpfel & Kevin F. O’Connell & Naoko Mizuno, 2025. "Structural insights into SSNA1 self-assembly and its microtubule binding for centriole maintenance," Nature Communications, Nature, vol. 16(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-62696-9
    DOI: 10.1038/s41467-025-62696-9
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