ArticleMolecular biology of the cell2013
Chlamydomonas ODA10 is a conserved axonemal protein that plays a unique role in outer dynein arm assembly.
Article in Molecular biology of the cell, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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23 citing papers in PubMed, 35 citations in OpenAlex.
- Culture method for promoting efficient ciliary growth in themicroPublication biology · 2026Article
- Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii.PLoS genetics · 2024Article
- Review
- Consensus nomenclature for dyneins and associated assembly factors.The Journal of cell biology · 2022Article
- Article
- Case Report: Identification of a NovelFrontiers in genetics · 2021Article
- Bi-allelic DNAH8 Variants Lead to Multiple Morphological Abnormalities of the Sperm Flagella and Primary Male Infertility.American journal of human genetics · 2020Article
- Identification of a frame shift mutation in the CCDC151 gene in a Han-Chinese family with Kartagener syndrome.Bioscience reports · 2020Article
- Asymmetries in the cilia ofPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020Review
- PKA, PP1, and DC1 phosphorylation mediate alcohol-induced ciliary dysfunction in Chlamydomonas reinhardtii.Alcohol (Fayetteville, N.Y.) · 2019Article
- In vivo analysis of outer arm dynein transport reveals cargo-specific intraflagellar transport properties.Molecular biology of the cell · 2018Article
- Ciliary Motility: Regulation of Axonemal Dynein Motors.Cold Spring Harbor perspectives in biology · 2017Review
- Evolution of Cilia.Cold Spring Harbor perspectives in biology · 2017Review
- Axonemal Dynein Arms.Cold Spring Harbor perspectives in biology · 2016Review
- Sperm dysfunction and ciliopathy.Reproductive medicine and biology · 2016Review
- Diverse Roles of Axonemal Dyneins in Drosophila Auditory Neuron Function and Mechanical Amplification in Hearing.Scientific reports · 2015Article
- Late steps in cytoplasmic maturation of assembly-competent axonemal outer arm dynein in Chlamydomonas require interaction of ODA5 and ODA10 in a complex.Molecular biology of the cell · 2015Article
- The oligomeric outer dynein arm assembly factor CCDC103 is tightly integrated within the ciliary axoneme and exhibits periodic binding to microtubules.The Journal of biological chemistry · 2015Article
- Chlamydomonas axonemal dynein assembly locus ODA8 encodes a conserved flagellar protein needed for cytoplasmic maturation of outer dynein arm complexes.Cytoskeleton (Hoboken, N.J.) · 2015Article
- Nonsense mutation in coiled-coil domain containing 151 gene (CCDC151) causes primary ciliary dyskinesia.Human mutation · 2014Article
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2 authors at 1 institution in 1 country.
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Abstract
Assembly of outer dynein arms (ODAs) requires multiple steps and involves multiple proteins in addition to dynein subunits. The Chlamydomonas ODA10, ODA5, and ODA8 loci genetically interact and are hypothesized to function as an axonemal accessory complex, but only ODA5p was previously characterized. We positionally cloned ODA10 and identified the gene by rescuing an oda10 mutant with a hemagglutinin-tagged cDNA. ODA10 sequence predicts a conserved coiled-coil protein homologous to mouse ccdc151. ODA10p is present in cytoplasm and flagella, remains axonemal after detergent treatment, and is extracted with 0.6 M NaCl. Both outer arm dynein and ODA10p rebound to the axonemes when desalted extracts are mixed with oda10-mutant axonemes. Sucrose gradient separation of these extracts shows that ODA10p sediments near the top of the gradient, not with 23S outer dynein arm proteins. Unexpectedly, dynein and ODA10p fractions are able to bind individually to oda10 axonemes. ODA10p is present on oda8-mutant flagella at wild-type levels. However, ODA10p does not assemble into oda5 flagella and is absent from oda5 cytoplasm, suggesting a necessity of ODA5p for stability of ODA10p in vivo. The results suggest that ODA10p does not function as a part of a traditionally defined docking complex.
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