The A-C linker controls centriole structural integrity and duplication

Lorène Bournonville, Marine. H. Laporte, Susanne Borgers, Paul Guichard () and Virginie Hamel ()
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Lorène Bournonville: Department of Molecular and Cellular Biology
Marine. H. Laporte: Department of Molecular and Cellular Biology
Susanne Borgers: Department of Molecular and Cellular Biology
Paul Guichard: Department of Molecular and Cellular Biology
Virginie Hamel: Department of Molecular and Cellular Biology

Nature Communications, 2025, vol. 16, issue 1, 1-19

Abstract: 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.

Date: 2025
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DOI: 10.1038/s41467-025-62154-6

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