ArticleProceedings of the National Academy of Sciences of the United States of America2024
Methylation of ciliary dynein motors involves the essential cytosolic assembly factor DNAAF3/PF22.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 8 citations in OpenAlex.
- Axonemal Dynein Visualized in Primary Cilia via Expansion Microscopy.Cytoskeleton (Hoboken, N.J.) · 2026Article
- Structural diversity and unity amongst axonemal dynein assembly factors.Journal of cell science · 2025Review
- Isoform-specific phosphorylation of axonemal dynein heavy chains.Molecular biology of the cell · 2025Article
- Phyloproteomics reveals conserved patterns of axonemal dynein methylation across the motile ciliated eukaryotes.Molecular biology of the cell · 2025Article
- The methylome of motile cilia.Molecular biology of the cell · 2024Article
- Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii.PLoS genetics · 2024Article
- Methylation of ciliary dynein motors involves the essential cytosolic assembly factor DNAAF3/PF22.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
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Authors and funding
4 authors at 2 institutions in 1 country.
Funding
Abstract
Axonemal dynein motors drive ciliary motility and can consist of up to twenty distinct components with a combined mass of ~2 MDa. In mammals, failure of dyneins to assemble within the axonemal superstructure leads to primary ciliary dyskinesia. Syndromic phenotypes include infertility, rhinitis, severe bronchial conditions, and situs inversus. Nineteen specific cytosolic factors (Dynein Axonemal Assembly Factors; DNAAFs) are necessary for axonemal dynein assembly, although the detailed mechanisms involved remain very unclear. Here, we identify the essential assembly factor DNAAF3 as a structural ortholog of S-adenosylmethionine-dependent methyltransferases. We demonstrate that dynein heavy chains, especially those forming the ciliary outer arms, are methylated on key residues within various nucleotide-binding sites and on microtubule-binding domain helices directly involved in the transition to low binding affinity. These variable modifications, which are generally missing in a
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