ArticlePLoS genetics2020
Mutations in PIH proteins MOT48, TWI1 and PF13 define common and unique steps for preassembly of each, different ciliary dynein.
Article in PLoS genetics, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
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Who cites it
15 citing papers in PubMed, 24 citations in OpenAlex.
- Culture method for promoting efficient ciliary growth in themicroPublication biology · 2026Article
- Phyloproteomics reveals conserved patterns of axonemal dynein methylation across the motile ciliated eukaryotes.Molecular biology of the cell · 2025Article
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- TCTEX1D2 is essential for sperm flagellum formation in mice.Scientific reports · 2025Article
- Inherently disordered regions of axonemal dynein assembly factors.Cytoskeleton (Hoboken, N.J.) · 2024Review
- Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii.PLoS genetics · 2024Article
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- Article
- FBB18 participates in preassembly of almost all axonemal dyneins independent of R2TP complex.PLoS genetics · 2022Article
- PCD Genes-From Patients to Model Organisms and Back to Humans.International journal of molecular sciences · 2022Review
- Strongly TruncatedFrontiers in genetics · 2022Article
- Cytoplasmic factories for axonemal dynein assembly.Journal of cell science · 2021Article
- Composition and function of ciliary inner-dynein-arm subunits studied in Chlamydomonas reinhardtii.Cytoskeleton (Hoboken, N.J.) · 2021Review
- Defects in the cytoplasmic assembly of axonemal dynein arms cause morphological abnormalities and dysmotility in sperm cells leading to male infertility.PLoS genetics · 2021Article
- Article
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Authors and funding
8 authors at 3 institutions in 2 countries.
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Abstract
Ciliary dyneins are preassembled in the cytoplasm before being transported into cilia, and a family of proteins containing the PIH1 domain, PIH proteins, are involved in the assembly process. However, the functional differences and relationships between members of this family of proteins remain largely unknown. Using Chlamydomonas reinhardtii as a model, we isolated and characterized two novel Chlamydomonas PIH preassembly mutants, mot48-2 and twi1-1. A new allele of mot48 (ida10), mot48-2, shows large defects in ciliary dynein assembly in the axoneme and altered motility. A second mutant, twi1-1, shows comparatively smaller defects in motility and dynein assembly. A double mutant mot48-2; twi1-1 displays greater reduction in motility and in dynein assembly compared to each single mutant. Similarly, a double mutant twi1-1; pf13 also shows a significantly greater defect in motility and dynein assembly than either parent mutant. Thus, MOT48 (IDA10), TWI1 and PF13 may define different steps, and have partially overlapping functions, in a pathway required for ciliary dynein preassembly. Together, our data suggest the three PIH proteins function in preassembly steps that are both common and unique for different ciliary dyneins.
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