ArticleMolecular biology of the cell2003
DC3, the 21-kDa subunit of the outer dynein arm-docking complex (ODA-DC), is a novel EF-hand protein important for assembly of both the outer arm and the ODA-DC.
Article in Molecular biology of the cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 44 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
44 citing papers in PubMed, 100 citations in OpenAlex.
- Proteins with proximal-distal asymmetries in axoneme localisation control flagellum beat frequency.Nature communications · 2025Article
- LRRC56 is an IFT cargo required for assembly of the distal dynein docking complex inMolecular biology of the cell · 2024Article
- Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii.PLoS genetics · 2024Article
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- Cytoplasmic factories for axonemal dynein assembly.Journal of cell science · 2021Article
- Heme-binding protein CYB5D1 is a radial spoke component required for coordinated ciliary beating.Proceedings of the National Academy of Sciences of the United States of America · 2021Article
- Structure of a microtubule-bound axonemal dynein.Nature communications · 2021Article
- Asymmetries in the cilia ofPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020Review
- Cilia Loss and Dynein Assembly Defects in Planaria Lacking an Outer Dynein Arm-Docking Complex Subunit.Zoological science · 2020Article
- Rare Human Diseases: Model Organisms in Deciphering the Molecular Basis of Primary Ciliary Dyskinesia.Cells · 2019Review
- Article
- Redox regulation of motile cilia in airway disease.Redox biology · 2019Review
- Review
- 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
- Inverse relationship of CaJournal of plant research · 2017Article
- Article
- Axonemal Dynein Arms.Cold Spring Harbor perspectives in biology · 2016Review
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
Abstract
The outer dynein arm-docking complex (ODA-DC) is a microtubule-associated structure that targets the outer dynein arm to its binding site on the flagellar axoneme (Takada et al. 2002. Mol. Biol. Cell 13, 1015-1029). The ODA-DC of Chlamydomonas contains three proteins, referred to as DC1, DC2, and DC3. We here report the isolation and sequencing of genomic and full-length cDNA clones encoding DC3. The sequence predicts a 21,341 Da protein with four EF-hands that is a member of the CTER (calmodulin, troponin C, essential and regulatory myosin light chains) group and is most closely related to a predicted protein from Plasmodium. The DC3 gene, termed ODA14, is intronless. Chlamydomonas mutants that lack DC3 exhibit slow, jerky swimming because of loss of some but not all outer dynein arms. Some outer doublet microtubules without arms had a "partial" docking complex, indicating that DC1 and DC2 can assemble in the absence of DC3. In contrast, DC3 cannot assemble in the absence of DC1 or DC2. Transformation of a DC3-deletion strain with the wild-type DC3 gene rescued both the motility phenotype and the structural defect, whereas a mutated DC3 gene was incompetent to rescue. The results indicate that DC3 is important for both outer arm and ODA-DC assembly.
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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.