ArticleCurrent biology : CB2014
Actin is required for IFT regulation in Chlamydomonas reinhardtii.
Article in Current biology : CB, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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47 citing papers in PubMed, 74 citations in OpenAlex.
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- Proteomic analysis reveals molecular changes following genetic engineering in Chlamydomonas reinhardtii.BMC microbiology · 2024Article
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- Disc and Actin Associated Protein 1 influences attachment in the intestinal parasite Giardia lamblia.PLoS pathogens · 2022Article
- The short flagella 1 (SHF1) gene inMolecular biology of the cell · 2022Article
- Identification of Actin Filament-Associated Proteins in Giardia lamblia.Microbiology spectrum · 2021Article
- Kinase-anchoring proteins in ciliary signal transduction.The Biochemical journal · 2021Review
- Finding your unique path in science.Molecular biology of the cell · 2020Article
- Scaling of Subcellular Structures.Annual review of cell and developmental biology · 2020Review
- Cleavage-furrow formation without F-actin inProceedings of the National Academy of Sciences of the United States of America · 2020Article
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10 authors at 4 institutions in 1 country.
Funding
Abstract
Assembly of cilia and flagella requires intraflagellar transport (IFT), a highly regulated kinesin-based transport system that moves cargo from the basal body to the tip of flagella [1]. The recruitment of IFT components to basal bodies is a function of flagellar length, with increased recruitment in rapidly growing short flagella [2]. The molecular pathways regulating IFT are largely a mystery. Because actin network disruption leads to changes in ciliary length and number, actin has been proposed to have a role in ciliary assembly. However, the mechanisms involved are unknown. In Chlamydomonas reinhardtii, conventional actin is found in both the cell body and the inner dynein arm complexes within flagella [3, 4]. Previous work showed that treating Chlamydomonas cells with the actin-depolymerizing compound cytochalasin D resulted in reversible flagellar shortening [5], but how actin is related to flagellar length or assembly remains unknown. Here we utilize small-molecule inhibitors and genetic mutants to analyze the role of actin dynamics in flagellar assembly in Chlamydomonas reinhardtii. We demonstrate that actin plays a role in IFT recruitment to basal bodies during flagellar elongation and that when actin is perturbed, the normal dependence of IFT recruitment on flagellar length is lost. We also find that actin is required for sufficient entry of IFT material into flagella during assembly. These same effects are recapitulated with a myosin inhibitor, suggesting that actin may act via myosin in a pathway by which flagellar assembly is regulated by flagellar length.
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