ArticleMolecular biology of the cell2005
The FLA3 KAP subunit is required for localization of kinesin-2 to the site of flagellar assembly and processive anterograde intraflagellar transport.
Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 70 papers.
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Who cites it
70 citing papers in PubMed, 142 citations in OpenAlex.
- Structure Makes a Difference: IFT Complex in Ciliary Function and Ciliopathy.Cytoskeleton (Hoboken, N.J.) · 2026Review
- Changes in the Adenylate Kinase Activity are Proportional to the ADP/ATP Ratio Upon Resorption and Regeneration of Chlamydomonas reinhardtii Flagella.Cell biochemistry and biophysics · 2025Article
- Regulation of kinesin-2 motility by its β-hairpin motif.Nature structural & molecular biology · 2025Article
- The intraflagellar transport cycle.Nature reviews. Molecular cell biology · 2025Review
- Distribution and bulk flow analyses of the intraflagellar transport (IFT) motor kinesin-2 support an "on-demand" model for Chlamydomonas ciliary length control.Cytoskeleton (Hoboken, N.J.) · 2024Article
- Review
- Deciphering vesicle-assisted transport mechanisms in cytoplasm to cilium trafficking.Frontiers in cellular neuroscience · 2024Review
- The ERK activator, BCI, inhibits ciliogenesis and causes defects in motor behavior, ciliary gating, and cytoskeletal rearrangement.Life science alliance · 2023Article
- Role of intraflagellar transport in transcriptional control during flagellar regeneration inMolecular biology of the cell · 2023Article
- The ciliary lumen accommodates passive diffusion and vesicle-assisted trafficking in cytoplasm-ciliary transport.Molecular biology of the cell · 2023Article
- Article
- Appearing and disappearing acts of cilia.Journal of biosciences · 2023Review
- Review
- The physiological cargo adaptor of kinesin-2 functions as an evolutionary conserved lockpick.Proceedings of the National Academy of Sciences of the United States of America · 2022Article
- Phosphoregulation of Kinesins Involved in Long-Range Intracellular Transport.Frontiers in cell and developmental biology · 2022Review
- Intraflagellar transport trains and motors: Insights from structure.Seminars in cell & developmental biology · 2020Review
- Functional exploration of heterotrimeric kinesin-II in IFT and ciliary length control ineLife · 2020Article
- Speed and Diffusion of Kinesin-2 Are Competing Limiting Factors in Flagellar Length-Control Model.Biophysical journal · 2020Article
- Kinesin-2 from C. reinhardtii Is an Atypically Fast and Auto-inhibited Motor that Is Activated by Heterotrimerization for Intraflagellar Transport.Current biology : CB · 2020Article
- FLS2 is a CDK-like kinase that directly binds IFT70 and is required for proper ciliary disassembly in Chlamydomonas.PLoS genetics · 2020Article
10 more citing papers are in PubMed but not listed here.
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Authors and funding
5 authors at 2 institutions in 1 country.
Funding
Abstract
Intraflagellar transport (IFT) is a bidirectional process required for assembly and maintenance of cilia and flagella. Kinesin-2 is the anterograde IFT motor, and Dhc1b/Dhc2 drives retrograde IFT. To understand how either motor interacts with the IFT particle or how their activities might be coordinated, we characterized a ts mutation in the Chlamydomonas gene encoding KAP, the nonmotor subunit of Kinesin-2. The fla3-1 mutation is an amino acid substitution in a conserved C-terminal domain. fla3-1 strains assemble flagella at 21 degrees C, but cannot maintain them at 33 degrees C. Although the Kinesin-2 complex is present at both 21 and 33 degrees C, the fla3-1 Kinesin-2 complex is not efficiently targeted to or retained in the basal body region or flagella. Video-enhanced DIC microscopy of fla3-1 cells shows that the frequency of anterograde IFT particles is significantly reduced. Anterograde particles move at near wild-type velocities, but appear larger and pause more frequently in fla3-1. Transformation with an epitope-tagged KAP gene rescues all of the fla3-1 defects and results in preferential incorporation of tagged KAP complexes into flagella. KAP is therefore required for the localization of Kinesin-2 at the site of flagellar assembly and the efficient transport of anterograde IFT particles within flagella.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.