ArticleThe Journal of biological chemistry2014
Insights into the structure and function of ciliary and flagellar doublet microtubules: tektins, Ca2+-binding proteins, and stable protofilaments.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
49 citing papers in PubMed, 85 citations in OpenAlex.
- Joubert syndrome 26 protein enforces compartmentalized motility of a ciliary kinesin.Proceedings of the National Academy of Sciences of the United States of America · 2025Article
- Evolutionary analysis of the Leishmania major orthologues for the newly identified cyclic AMP response proteins.Archives of microbiology · 2025Article
- Genetic Animal Models of Idiopathic Generalized Epilepsies: What Can We Learn from Them?Biomedicines · 2025Review
- Tubulin Polymerization Promoting Proteins: Functional Diversity With Implications in Neurological Disorders.Journal of neuroscience research · 2025Review
- Trypanosome doublet microtubule structures reveal flagellum assembly and motility mechanisms.Science (New York, N.Y.) · 2025Article
- Centriole and transition zone structures in photoreceptor cilia revealed by cryo-electron tomography.Life science alliance · 2024Article
- In-cell structural insight into the stability of sperm microtubule doublet.Cell discovery · 2023Article
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- Molecular Markers: A New Paradigm in the Prediction of Sperm Freezability.International journal of molecular sciences · 2023Review
- Aurora A Kinase (AURKA) is required for male germline maintenance and regulates sperm motility in the mouse.Biology of reproduction · 2021Article
- Structure and dynamics of photoreceptor sensory cilia.Pflugers Archiv : European journal of physiology · 2021Review
- Clinical and genetic heterogeneity of primary ciliopathies (Review).International journal of molecular medicine · 2021Review
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- Acetylation/deacetylation and microtubule associated proteins influence flagellar axonemal stability and sperm motility.Bioscience reports · 2020Article
- Disc-associated proteins mediate the unusual hyperstability of the ventral disc inJournal of cell science · 2020Article
- In situ structure determination at nanometer resolution using TYGRESS.Nature methods · 2020Article
- Microtubule number and length determine cellular shape and function in Plasmodium.The EMBO journal · 2019Article
- Review
- PACRG and FAP20 form the inner junction of axonemal doublet microtubules and regulate ciliary motility.Molecular biology of the cell · 2019Article
Corrections and comments
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Authors and funding
8 authors at 3 institutions in 2 countries.
Funding
Abstract
Cilia and flagella are conserved, motile, and sensory cell organelles involved in signal transduction and human disease. Their scaffold consists of a 9-fold array of remarkably stable doublet microtubules (DMTs), along which motor proteins transmit force for ciliary motility and intraflagellar transport. DMTs possess Ribbons of three to four hyper-stable protofilaments whose location, organization, and specialized functions have been elusive. We performed a comprehensive analysis of the distribution and structural arrangements of Ribbon proteins from sea urchin sperm flagella, using quantitative immunobiochemistry, proteomics, immuno-cryo-electron microscopy, and tomography. Isolated Ribbons contain acetylated α-tubulin, β-tubulin, conserved protein Rib45, >95% of the axonemal tektins, and >95% of the calcium-binding proteins, Rib74 and Rib85.5, whose human homologues are related to the cause of juvenile myoclonic epilepsy. DMTs contain only one type of Ribbon, corresponding to protofilaments A11-12-13-1 of the A-tubule. Rib74 and Rib85.5 are associated with the Ribbon in the lumen of the A-tubule. Ribbons contain a single ∼5-nm wide filament, composed of equimolar tektins A, B, and C, which interact with the nexin-dynein regulatory complex. A summary of findings is presented, and the functions of Ribbon proteins are discussed in terms of the assembly and stability of DMTs, ciliary motility, and other microtubule systems.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.