ArticleThe Journal of cell biology1997
Phosphoregulation of an inner dynein arm complex in Chlamydomonas reinhardtii is altered in phototactic mutant strains.
Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 78 papers.
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Who cites it
78 citing papers in PubMed.
- Doublet microtubule-associated tektins and enzymes differentially regulate sperm flagellar integrity and motility.Nature communications · 2026Article
- Mouse radial spoke 3 is a metabolic and regulatory hub in cilia.Nature structural & molecular biology · 2025Article
- 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
- Defective I1 dynein inmicroPublication biology · 2025Article
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- The MBO2/FAP58 heterodimer stabilizes assembly of inner arm dyneinMolecular biology of the cell · 2024Article
- Perspectives on Principles of Cellular Behavior from the Biophysics of Protists.Integrative and comparative biology · 2023Review
- Article
- Article
- Structural organization of the intermediate and light chain complex of Chlamydomonas ciliary I1 dynein.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2021Article
- Composition and function of ciliary inner-dynein-arm subunits studied in Chlamydomonas reinhardtii.Cytoskeleton (Hoboken, N.J.) · 2021Review
- A dynein-associated photoreceptor protein prevents ciliary acclimation to blue light.Science advances · 2021Article
- Speed and Diffusion of Kinesin-2 Are Competing Limiting Factors in Flagellar Length-Control Model.Biophysical journal · 2020Article
- Asymmetries in the cilia ofPhilosophical transactions of the Royal Society of London. Series B, Biological sciences · 2020Review
- PACRG and FAP20 form the inner junction of axonemal doublet microtubules and regulate ciliary motility.Molecular biology of the cell · 2019Article
- Vertebrate Dynein-f depends on Wdr78 for axonemal localization and is essential for ciliary beat.Journal of molecular cell biology · 2019Article
- The I1 dynein-associated tether and tether head complex is a conserved regulator of ciliary motility.Molecular biology of the cell · 2018Article
- A microtubule-dynein tethering complex regulates the axonemal inner dynein f (I1).Molecular biology of the cell · 2018Article
- The Bardet-Biedl syndrome protein complex is an adapter expanding the cargo range of intraflagellar transport trains for ciliary export.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
18 more citing papers are in PubMed but not listed here.
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2 authors.
Funding
Abstract
To gain a further understanding of axonemal dynein regulation, mutant strains of Chlamydomonas reinhardtii that had defects in both phototactic behavior and flagellar motility were identified and characterized. ptm1, ptm2, and ptm3 mutant strains exhibited motility phenotypes that resembled those of known inner dynein arm region mutant strains, but did not have biochemical or genetic phenotypes characteristic of other inner dynein arm mutations. Three other mutant strains had defects in the f class of inner dynein arms. Dynein extracts from the pf9-4 strain were missing the entire f complex. Strains with mutations in pf9/ida1, ida2, or ida3 failed to assemble the f dynein complex and did not exhibit phototactic behavior. Fractionated dynein from mia1-1 and mia2-1 axonemes exhibited a novel f class inner dynein arm biochemical phenotype; the 138-kD f intermediate chain was present in altered phosphorylation forms. In vitro axonemal dynein activity was reduced by the mia1-1 and mia2-1 mutations. The addition of kinase inhibitor restored axonemal dynein activity concomitant with the dephosphorylation of the 138-kD f intermediate chain. Dynein extracts from uni1-1 axonemes, which specifically assemble only one of the two flagella, contained relatively high levels of the altered phosphorylation forms of the 138-kD intermediate chain. We suggest that the f dynein complex may be phosphoregulated asymmetrically between the two flagella to achieve phototactic turning.
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