ArticleJournal of cell science2012
Structure-function relationship of the Polo-like kinase in Trypanosoma brucei.
Article in Journal of cell science, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 26 citations in OpenAlex.
- An independently tunable dual control system for RNAi complementation in Trypanosoma brucei.PloS one · 2025Article
- Divergent polo boxes in KKT2 bind KKT1 to initiate the kinetochore assembly cascade inMolecular biology of the cell · 2022Article
- Polo-like kinase and Aurora B kinase phosphorylate and cooperate with the CIF1-CIF2 complex to promote cytokinesis initiation inOpen biology · 2022Article
- The kinetoplastid-specific phosphatase KPP1 attenuates PLK activity to facilitate flagellum inheritance inScience signaling · 2021Article
- Polo-like kinase in trypanosomes: an odd member out of the Polo family.Open biology · 2020Article
- A DNA polymerization-independent role for mitochondrial DNA polymerase I-like protein C in African trypanosomes.Journal of cell science · 2020Article
- Flagellum inheritance inThe Journal of biological chemistry · 2018Article
- Functional analyses of the CIF1-CIF2 complex in trypanosomes identify the structural motifs required for cytokinesis.Journal of cell science · 2017Article
- A functional analysis of TOEFAZ1 uncovers protein domains essential for cytokinesis inJournal of cell science · 2017Article
- CRL4WDR1 Controls Polo-like Kinase Protein Abundance to Promote Bilobe Duplication, Basal Body Segregation and Flagellum Attachment in Trypanosoma brucei.PLoS pathogens · 2017Article
- Divergent polo box domains underpin the unique kinetoplastid kinetochore.Open biology · 2016Article
- A Novel Basal Body Protein That Is a Polo-like Kinase Substrate Is Required for Basal Body Segregation and Flagellum Adhesion in Trypanosoma brucei.The Journal of biological chemistry · 2015Article
- Proteomic identification of novel cytoskeletal proteins associated with TbPLK, an essential regulator of cell morphogenesis in Trypanosoma brucei.Molecular biology of the cell · 2015Article
- New insights into the molecular mechanisms of mitosis and cytokinesis in trypanosomes.International review of cell and molecular biology · 2014Review
- The cooperative roles of PHO80-like cyclins in regulating the G1/S transition and posterior cytoskeletal morphogenesis in Trypanosoma brucei.Molecular microbiology · 2013Article
- Polo-like kinase phosphorylation of bilobe-resident TbCentrin2 facilitates flagellar inheritance in Trypanosoma brucei.Molecular biology of the cell · 2013Article
- An analogue-sensitive approach identifies basal body rotation and flagellum attachment zone elongation as key functions of PLK in Trypanosoma brucei.Molecular biology of the cell · 2013Article
- Regulation of the cell division cycle in Trypanosoma brucei.Eukaryotic cell · 2012Review
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
Abstract
Polo-like kinases (Plks) play multiple roles in mitosis and cytokinesis in eukaryotes and are characterized by the C-terminal Polo-box domain (PBD), which is implicated in binding to Plk substrates, targeting Plk and regulating Plk activity. The Plk homolog in Trypanosoma brucei (TbPLK) possesses a similar architecture, but it lacks the crucial residues involved in substrate binding and regulates cytokinesis but not mitosis. Little is known about the regulation of TbPLK and the role of the PBD in TbPLK localization and function. Here, we addressed the requirement of the kinase activity and the PBD for TbPLK localization and function through coupling RNAi of endogenous TbPLK with ectopic expression of TbPLK mutants. We demonstrate that the kinase activity and phosphorylation of two threonine residues, Thr198 and Thr202, in the activation loop (T-loop) of the kinase domain are essential for TbPLK function but not for TbPLK localization. Deletion of the PBD abolishes TbPLK localization, but the PBD itself is not correctly targeted, indicating that TbPLK localization requires both the PBD and the kinase domain. Surprisingly, the kinase domain of TbPLK, but not the PBD, binds to its substrates TbCentrin2 and p110, suggesting that TbPLK might interact with its substrate through different mechanisms. Finally, the PBD interacts with the kinase domain of TbPLK and inhibits its activity, and this inhibition is relieved when Thr198 is phosphorylated. Together, these results suggest an essential role of T-loop phosphorylation in TbPLK activation and crucial roles of the PBD in regulating TbPLK activity and localization.
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