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The A-C linker controls centriole structural integrity and duplication

Author

Listed:
  • Lorène Bournonville

    (Department of Molecular and Cellular Biology)

  • Marine. H. Laporte

    (Department of Molecular and Cellular Biology
    Institut NeuroMyoGène)

  • Susanne Borgers

    (Department of Molecular and Cellular Biology)

  • Paul Guichard

    (Department of Molecular and Cellular Biology)

  • Virginie Hamel

    (Department of Molecular and Cellular Biology)

Abstract

Centrioles are evolutionarily conserved barrel-shaped organelles playing crucial roles in cell division and ciliogenesis. These functions are underpinned by specific structural sub-elements whose functions have been under investigation since many years. The A-C linker structure, connecting adjacent microtubule triplets in the proximal region, has remained unexplored due to its unknown composition. Here, using ultrastructure expansion microscopy, we characterized two recently identified A-C linker proteins, CCDC77 and WDR67, and discovered MIIP as an additional A-C linker protein. Our findings reveal that these proteins localize between microtubule triplets at the A-C linker, forming a complex. Depletion of A-C linker components disrupt microtubule triplet cohesion, leading to breakage at the proximal end. Co-removal of the A-C linker and the inner scaffold demonstrates their joint role in maintaining centriole architecture. Moreover, we uncover an unexpected function of the A-C linker in centriole duplication through torus regulation, underscoring the interplay between these protein modules.

Suggested Citation

  • Lorène Bournonville & Marine. H. Laporte & Susanne Borgers & Paul Guichard & Virginie Hamel, 2025. "The A-C linker controls centriole structural integrity and duplication," Nature Communications, Nature, vol. 16(1), pages 1-19, December.
    • Handle: RePEc:nat:natcom:v:16:y:2025:i:1:d:10.1038_s41467-025-62154-6
    DOI: 10.1038/s41467-025-62154-6
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