ArticleFEBS letters2013
Protein-protein interactions between intermediate chains and the docking complex of Chlamydomonas flagellar outer arm dynein.
Article in FEBS letters, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 19 citations in OpenAlex.
- Cytoplasmic preassembly of the flagellar outer dynein arm 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
- Homozygous mutation inFrontiers in endocrinology · 2022Article
- Structure of a microtubule-bound axonemal dynein.Nature communications · 2021Article
- 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
- 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
- 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 ciliary inner dynein arm, I1 dynein, is assembled in the cytoplasm and transported by IFT before axonemal docking.Cytoskeleton (Hoboken, N.J.) · 2014Article
- Cooperative binding of the outer arm-docking complex underlies the regular arrangement of outer arm dynein in the axoneme.Proceedings of the National Academy of Sciences of the United States of America · 2014Article
Corrections and comments
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Authors and funding
5 authors at 4 institutions in 2 countries.
Funding
Abstract
Outer arm dynein (OAD) is bound to specific loci on outer-doublet-microtubules by interactions at two sites: via intermediate chain 1 (IC1) and the outer dynein arm docking complex (ODA-DC). Studies using Chlamydomonas mutants have suggested that the individual sites have rather weak affinities for microtubules, and therefore strong OAD attachment to microtubules is achieved by their cooperation. To test this idea, we examined interactions between IC1, IC2 (another intermediate chain) and ODA-DC using recombinant proteins. Recombinant IC1 and IC2 were found to form a 1:1 complex, and this complex associated with ODA-DC in vitro. Binding of IC1 to mutant axonemes revealed that there are specific binding sites for IC1. From these data, we propose a novel model of OAD-outer doublet association.
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