ArticleThe Journal of cell biology1995
The 78,000-M(r) intermediate chain of Chlamydomonas outer arm dynein is a microtubule-binding protein.
Article in The Journal of cell biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
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Who cites it
25 citing papers in PubMed.
- Gene dosage of independent dynein arm motor preassembly factors influences cilia assembly in Chlamydomonas reinhardtii.PLoS genetics · 2024Article
- Structure of a microtubule-bound axonemal dynein.Nature communications · 2021Article
- Structure and function of outer dynein arm intermediate and light chain complex.Molecular biology of the cell · 2016Article
- 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
- Protein-protein interactions between intermediate chains and the docking complex of Chlamydomonas flagellar outer arm dynein.FEBS letters · 2013Article
- ODA16p, a Chlamydomonas flagellar protein needed for dynein assembly.Molecular biology of the cell · 2005Article
- The LC7 light chains of Chlamydomonas flagellar dyneins interact with components required for both motor assembly and regulation.Molecular biology of the cell · 2004Article
- A sperm-associated WD repeat protein orthologous to Chlamydomonas PF20 associates with Spag6, the mammalian orthologue of Chlamydomonas PF16.Molecular and cellular biology · 2002Article
- Backbone dynamics of the 8 kDa dynein light chain dimer reveals molecular basis of the protein's functional diversity.Journal of biomolecular NMR · 2002Article
- The outer dynein arm-docking complex: composition and characterization of a subunit (oda1) necessary for outer arm assembly.Molecular biology of the cell · 2002Article
- The human dynein intermediate chain 2 gene (DNAI2): cloning, mapping, expression pattern, and evaluation as a candidate for primary ciliary dyskinesia.Human genetics · 2000Article
- Loss-of-function mutations in a human gene related to Chlamydomonas reinhardtii dynein IC78 result in primary ciliary dyskinesia.American journal of human genetics · 1999Article
- LC2, the chlamydomonas homologue of the t complex-encoded protein Tctex2, is essential for outer dynein arm assembly.Molecular biology of the cell · 1999Article
- Domains in the 1alpha dynein heavy chain required for inner arm assembly and flagellar motility in Chlamydomonas.The Journal of cell biology · 1999Article
- The Chlamydomonas IDA7 locus encodes a 140-kDa dynein intermediate chain required to assemble the I1 inner arm complex.Molecular biology of the cell · 1998Article
- The Mr 140,000 intermediate chain of Chlamydomonas flagellar inner arm dynein is a WD-repeat protein implicated in dynein arm anchoring.Molecular biology of the cell · 1998Article
- The role of preassembled cytoplasmic complexes in assembly of flagellar dynein subunits.Molecular biology of the cell · 1998Article
- Identification of the t complex-encoded cytoplasmic dynein light chain tctex1 in inner arm I1 supports the involvement of flagellar dyneins in meiotic drive.The Journal of cell biology · 1998Article
- A Chlamydomonas homologue of the putative murine t complex distorter Tctex-2 is an outer arm dynein light chain.The Journal of cell biology · 1997Article
- The Chlamydomonas reinhardtii ODA3 gene encodes a protein of the outer dynein arm docking complex.The Journal of cell biology · 1997Article
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4 authors.
Funding
Abstract
A previous study (King et al., 1991. J. Biol. Chem. 266:8401-8407) showed that the 78,000-M(r) intermediate chain (IC78) from the Chlamydomonas outer arm dynein is in direct contact with alpha-tubulin in situ, suggesting that this protein may be involved in binding the dynein to the doublet microtubules. Molecular genetic analysis of this chain recently demonstrated that it is a WD repeat protein essential for outer arm assembly (Wilkerson et al., 1995.J. Cell Biol. 129:169-178). We have now transcribed and translated IC78 in vitro, and demonstrate that this molecule binds axonemes and microtubules, whereas a homologous protein (the 69,000-M(r) intermediate chain [IC69] of Chlamydomonas outer arm dynein) does not. Thus, IC78 is a bona fide microtubule-binding protein. Taken together with the previous results, these findings indicate that IC78 is likely to provide at least some of the adhesive force that holds the dynein to the doublet microtubule, and support the general hypothesis that the dynein intermediate chains are involved in targeting different dyneins to the specific cell organelles with which they associate. Analysis of the binding activities of various IC78 deletion constructs translated in vitro identified discrete regions of IC78 that affected the binding to microtubules; two of these regions are specifically missing in IC69. Previous studies also showed that IC78 is in direct contact with IC69; the current work indicates that the region of IC78 that mediates this interaction is coincident with two of IC78's WD repeats. This supports the hypothesis that these repeats are involved in protein-protein interactions within the dynein complex.
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