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Cited by 10Microtubule and mitosis dynamicsProtein Structure and DynamicsGenetic and Kidney Cyst Diseases

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

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Agostini, Lorenzo, Pfister, Jason A., Basnet, Nirakar, Ding, Jienyu, Zhang, Rui, Biertümpfel, Christian, O’Connell, Kevin F., Mizuno, Naoko·2025·Nature Communications
DOI 10.1038/s41467-025-62696-9PMC PMC12350680

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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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Metadata

Authors
Agostini, L., Pfister, J. A., Basnet, N., Ding, J., Zhang, R., Biertümpfel, C., O’Connell, K. F., & Mizuno, N.
Affiliations
  • National Institutes of Health (US)
  • Washington University in St. Louis (US)
Corresponding author
  • Biertümpfel, Christian
  • O’Connell, Kevin F.
  • Mizuno, Naoko
ORCID
Venue
Nature Communications
Publisher
Springer Science and Business Media LLC
Published
2025-08-13
Volume
16
Issue
1
Pages
7512-7512
ISSN
2041-1723 (ISSN-L)
DOI
10.1038/s41467-025-62696-9
PMC
PMC12350680
OpenAlex
W4413116633
Cited by
10
References
1
Citations by year
2026: 2 · 2025: 7
FWCI
4.49
Type
journal article
Language
en
Open access
Licence
Locations
  • Nature Communications (publishedVersion, cc-by)
  • bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, public-domain)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • PubMed Central (submittedVersion, public-domain)
  • Digital Commons@Becker (Washington University School of Medicine) (submittedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
Funders
U.S. Department of Health & Human Services | NIH | National Heart, Lung, and Blood Institute (1ZIAHL006264)
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Microtubule and mitosis dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Genetics › Genetic and Kidney Cyst Diseases
Keywords
fibrillar proteins, protein self-assembly, microtubule binding, coiled coil, microtubule remodeling, multipolar spindles, embryo viability, cell division regulation, Caenorhabditis elegans

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