ArticleNature structural & molecular biology2025
A network of interacting ciliary tip proteins with opposing activities imparts slow and processive microtubule growth.
Article in Nature structural & molecular biology, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 12 papers.
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Who cites it
12 citing papers in PubMed.
- Taxane-induced conformational changes in the microtubule lattice activate GEF-H1-dependent RhoA signalling.Nature cell biology · 2026Article
- Microtubule binding protein Togaram1 is required for proper development of mammalian forebrain and neural primary cilia.Developmental biology · 2026Article
- Towards a systems-level view of the microtubule cytoskeleton and its functions in physiology and disease.Nature reviews. Molecular cell biology · 2026Review
- Primary cilium disassembly - from mechanisms to roles in physiology and disease.Journal of cell science · 2026Review
- Togaram Ensures Axial Alignment of the Sperm Neck.bioRxiv : the preprint server for biology · 2026Article
- Primary cilia function as hubs for signal transduction.Cell & bioscience · 2025Review
- CEP290 deficiency disrupts ciliary axonemal architecture in human iPSC-derived brain organoids.Journal of cell science · 2025Article
- Advances in ciliary proteomics - towards cracking the hidden proteome code of cilia.Journal of cell science · 2025Review
- CCDC66 regulation of cytoskeleton and cilia stability is important for signaling and epithelial organization.PLoS biology · 2025Article
- Microtubule dynamics are defined by conformations and stability of clustered protofilaments.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Left-right cortical interactions drive intracellular pattern formation in the ciliate Tetrahymena.PLoS genetics · 2025Article
- Centriolar cap proteins CP110 and CPAP control slow elongation of microtubule plus ends.The Journal of cell biology · 2025Article
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8 authors.
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Abstract
Cilia are motile or sensory organelles present on many eukaryotic cells. Their formation and function rely on axonemal microtubules, which exhibit very slow dynamics, but the underlying mechanisms are largely unexplored. Here we reconstituted in vitro the individual and collective activities of the ciliary tip module proteins CEP104, CSPP1, TOGARAM1, ARMC9 and CCDC66, which interact with each other and with microtubules and, when mutated in humans, cause ciliopathies such as Joubert syndrome. We show that CEP104, a protein with a tubulin-binding TOG domain, and its luminal partner CSPP1 inhibit microtubule growth and shortening. Another TOG-domain protein, TOGARAM1, overcomes growth inhibition imposed by CEP104 and CSPP1. CCDC66 and ARMC9 do not affect microtubule dynamics but act as scaffolds for their partners. Cryo-electron tomography demonstrated that, together, ciliary tip module members form plus-end-specific cork-like structures that reduce protofilament flaring. The combined effect of these proteins is very slow processive microtubule elongation, which recapitulates axonemal dynamics in cells.
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