ArticleThe Journal of biological chemistry2015
The oligomeric outer dynein arm assembly factor CCDC103 is tightly integrated within the ciliary axoneme and exhibits periodic binding to microtubules.
Article in The Journal of biological chemistry, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 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
32 citing papers in PubMed, 58 citations in OpenAlex.
- DNAAF19-RUVBL1/2 complex recruits multiple adaptors to promote dynein arm assembly.Proceedings of the National Academy of Sciences of the United States of America · 2026Article
- Structural diversity and unity amongst axonemal dynein assembly factors.Journal of cell science · 2025Review
- A novel missense mutation of CCDC34 causes male infertility with oligoasthenoteratozoospermia in a consanguineous Pakistani family.Asian journal of andrology · 2024Article
- Gene expression, evolution, and the genetics of electrosensing in the smalltooth sawfish,Ecology and evolution · 2024Article
- Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii.PLoS genetics · 2024Article
- LRRC6 regulates biogenesis of motile cilia by aiding FOXJ1 translocation into the nucleus.Cell communication and signaling : CCS · 2023Article
- Review
- Morphological and Molecular Bases of Male Infertility: A Closer Look at Sperm Flagellum.Genes · 2023Review
- Case report: The CCDC103 variant causes ultrastructural sperm axonemal defects and total sperm immotility in a professional athlete without primary ciliary diskinesia.Frontiers in genetics · 2023Article
- CCDC103 as a Prognostic Biomarker Correlated with Tumor Progression and Immune Infiltration in Glioma.OncoTargets and therapy · 2023Article
- Cilia proteins getting to work - how do they commute from the cytoplasm to the base of cilia?Journal of cell science · 2022Review
- Flagellar energy costs across the tree of life.eLife · 2022Article
- PCD Genes-From Patients to Model Organisms and Back to Humans.International journal of molecular sciences · 2022Review
- Ccdc103 promotes myeloid cell proliferation and migration independent of motile cilia.Disease models & mechanisms · 2021Article
- Mutations in PIH proteins MOT48, TWI1 and PF13 define common and unique steps for preassembly of each, different ciliary dynein.PLoS genetics · 2020Article
- RPAP3 C-Terminal Domain: A Conserved Domain for the Assembly of R2TP Co-Chaperone Complexes.Cells · 2020Review
- Cilia Loss and Dynein Assembly Defects in Planaria Lacking an Outer Dynein Arm-Docking Complex Subunit.Zoological science · 2020Article
- The outer dynein arm assembly factor CCDC103 forms molecular scaffolds through multiple self-interaction sites.Cytoskeleton (Hoboken, N.J.) · 2020Article
- Rare Human Diseases: Model Organisms in Deciphering the Molecular Basis of Primary Ciliary Dyskinesia.Cells · 2019Review
- Characterization of CCDC103 expression profiles: further insights in primary ciliary dyskinesia and in human reproduction.Journal of assisted reproduction and genetics · 2019Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
CCDC103 is an ∼29-kDa protein consisting of a central RPAP3_C domain flanked by N- and C-terminal coiled coils. Defects in CCDC103 lead to primary ciliary dyskinesia caused by the loss of outer dynein arms. This protein is present along the entire length of the ciliary axoneme and does not require other dynein or docking complex components for its integration. Unlike other known dynein assembly factors within the axoneme, CCDC103 is not solubilized by 0.6 M NaCl and requires more chaotropic conditions, such as 0.5 M KI. Alternatively, it can be extracted using 0.3% sarkosyl. CCDC103 forms stable dimers and other oligomers in solution through interactions involving the central domain. The smallest particle observed by dynamic light scattering has a hydrodynamic diameter of ∼25 nm. Furthermore, CCDC103 binds microtubules directly, forming ∼9-nm diameter particles that exhibit a 12-nm spacing on the microtubule lattice, suggesting that there may be two CCDC103 units per outer arm dynein repeat. Although the outer dynein arm docking complex is necessary to form arrays of dyneins along microtubules, it is not sufficient to set up a single array in a precise location on each axonemal doublet. We propose that CCDC103 helps generate a high-affinity site on the doublets for outer arm assembly, either through direct interactions or indirectly, perhaps by modifying the underlying microtubule lattice.
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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.