ArticleScientific reports2018
Identification of a flagellar protein implicated in the gravitaxis in the flagellate Euglena gracilis.
Article in Scientific reports, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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11 citing papers in PubMed, 18 citations in OpenAlex.
- Acceleration and Light-Induced Changes in Cytosolic cAMP Concentration inBiomolecules · 2026Article
- Euglena gracilis Subcellular Fractionation.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Engineering Wax Ester Composition in Euglena gracilis Using Genome Editing.Methods in molecular biology (Clifton, N.J.) · 2026Article
- Visualisation ofLife science alliance · 2025Article
- Review
- Molecular Cross-Talk between Gravity- and Light-Sensing Mechanisms inInternational journal of molecular sciences · 2022Article
- A Synthetic Biology Perspective on the Bioengineering Tools for an Industrial Microalga:Frontiers in bioengineering and biotechnology · 2022Review
- Temporal Evolution of the Gravitaxis ofPlants (Basel, Switzerland) · 2021Article
- The morbid genome of ciliopathies: an update.Genetics in medicine : official journal of the American College of Medical Genetics · 2020Article
- Changes of Gene Expression in Euglena gracilis Obtained During the 29Scientific reports · 2019Article
- Lessons Learned from Large-Scale, First-Tier Clinical Exome Sequencing in a Highly Consanguineous Population.American journal of human genetics · 2019Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Flagellated cells are of great evolutionary importance across animal and plant species. Unlike higher plants, flagellated cells are involved in reproduction of macro-algae as well as in early diverging land plants. Euglena gracilis is an emerging flagellated model organism. The current study reports that a specific calmodulin (CaM2) involved in gravitaxis of E. gracilis interacts with an evolutionary conserved flagellar protein, EgPCDUF4201. The subsequent molecular analysis showed clearly that EgPCDUF4201 is also involved in gravitaxis. We performed subcellular localization of CaM2 using immunoblotting and indirect immunofluorescence. By employing yeast two-hybrid screen, EgPCDUF4201 was identified as an interaction partner of CaM2. The C-terminus of EgPCDUF4201 is responsible for the interaction with CaM2. Silencing of N- and C-terminus of EgPCDUF4201 using RNAi resulted in an impaired gravitaxis. Moreover, indirect immunofluorescence assay showed that EgPCDUF4201 is a flagella associated protein. The current study specifically addressed some important questions regarding the signal transduction chain of gravitaxis in E. gracilis. Besides the fact that it improved the current understanding of gravity sensing mechanisms in E. gracilis, it also gave rise to several interesting research questions regarding the function of the domain of unknown function 4201 in flagellated cells.
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