ArticleNature communications2025
The A-C linker controls centriole structural integrity and duplication.
Article in Nature communications, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed.
- Microtubule-Associated Proteins: From Dynamic Regulation of Microtubules to Cellular Architecture.Cells · 2026Review
- Molecular architecture of the ciliary base in mammalian multiciliated cells.bioRxiv : the preprint server for biology · 2026Article
- Critical constituents and assembly principles of centriole biogenesis in human cells.Nature reviews. Molecular cell biology · 2026Review
- The γ-TuRC: mastermind of multipurpose actions at the centrosome.Cellular and molecular life sciences : CMLS · 2026Review
- Centrin-POC5 inner scaffold provides distal centriole integrity for sperm flagellar assembly.Science advances · 2025Article
- The luminal ring protein C2CD3 acts as a radial in-to-out organizer of the distal centriole and appendages.PLoS biology · 2025Article
- Advances in high-resolution imaging of centrioles and cilia.Journal of cell science · 2025Review
- Structure and assembly of the A-C linker connecting microtubule triplets in centrioles.Science advances · 2025Article
- A delta-tubulin/epsilon-tubulin/Ted protein complex is required for centriole architecture.eLife · 2025Article
Corrections and comments
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Authors and funding
5 authors.
Funding
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.
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Registered trials
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