ArticleThe Journal of cell biology2024
Poc1 bridges basal body inner junctions to promote triplet microtubule integrity and connections.
Article in The Journal of cell biology, 2024. 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.
- Ana1/Cep295 regulates centriole elongation via Cep135 and microtubules.The Journal of cell biology · 2026Article
- Big1 is a cell-cycle regulator linking cell size to basal body number in Tetrahymena thermophila.Current biology : CB · 2026Article
- Loss-of-function variants in SAXO6, encoding a microtubule inner protein of photoreceptor cilia, cause a late-onset retinal dystrophy.American journal of human genetics · 2026Article
- Resolving structural heterogeneity in situ through cryogenic electron tomography.Current opinion in structural biology · 2026Review
- Centrin-POC5 inner scaffold provides distal centriole integrity for sperm flagellar assembly.Science advances · 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
- The A-C linker controls centriole structural integrity and duplication.Nature communications · 2025Article
- A ternary complex of MIPs in the A-tubule of basal bodies and axonemes depends on RIB22 and the EF-hand domain of RIB72A inMolecular biology of the cell · 2025Article
- An interaction network of inner centriole proteins organised by POC1A-POC1B heterodimer crosslinks ensures centriolar integrity.Nature communications · 2024Article
- The Structure of Cilium Inner Junctions Revealed by Electron Cryo-tomography.bioRxiv : the preprint server for biology · 2024Article
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Abstract
Basal bodies (BBs) are conserved eukaryotic structures that organize cilia. They are comprised of nine, cylindrically arranged, triplet microtubules (TMTs) connected to each other by inter-TMT linkages which stabilize the structure. Poc1 is a conserved protein important for BB structural integrity in the face of ciliary forces transmitted to BBs. To understand how Poc1 confers BB stability, we identified the precise position of Poc1 in the Tetrahymena BB and the effect of Poc1 loss on BB structure. Poc1 binds at the TMT inner junctions, stabilizing TMTs directly. From this location, Poc1 also stabilizes inter-TMT linkages throughout the BB, including the cartwheel pinhead and the inner scaffold. The full localization of the inner scaffold protein Fam161A requires Poc1. As ciliary forces are increased, Fam161A is reduced, indicative of a force-dependent molecular remodeling of the inner scaffold. Thus, while not essential for BB assembly, Poc1 promotes BB interconnections that establish an architecture competent to resist ciliary forces.
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