Evidence map›Paper›PMID 17662039›Full record

ArticleMolecular microbiology2007

Trypanosoma brucei Polo-like kinase is essential for basal body duplication, kDNA segregation and cytokinesis.

Tansy C Hammarton, Susanne Kramer, Laurence Tetley, Michael Boshart, Jeremy C Mottram

Open access · bronzeAbstract read
In one paragraph

Article in Molecular microbiology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 74 papers.

0numbers the graph read from it
0cells of the map it votes in
74citing papers in PubMed
3.1field-weighted citation impact, top 8% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

74 citing papers in PubMed, 109 citations in OpenAlex.

  1. Article
  2. A limitation lifted: A conditional knockdown system reveals essential roles for Polo-like kinase and Aurora kinase 1 inProceedings of the National Academy of Sciences of the United States of America · 2025
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  6. FAZ assembly in bloodstream formMolecular biology of the cell · 2023
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14 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

5 authors at 3 institutions in 2 countries.

Tansy C HammartonInfection and Immunity, Wellcome Centre for Molecular Parasitology, University of Glasgow, Biomedical Research Centre, 120 University Place, Glasgow G12 8TA, UK. t.hammarton@bio.gla.ac.uk
Susanne Kramer
Laurence Tetley
Michael Boshart
Jeremy C Mottram
LMU Klinikum · DEWellcome Centre for Molecular Parasitology · GBUniversity of Glasgow · GB

Funding

Medical Research Council G120/1001Wellcome Trust 072031
6 · The paper itself

Abstract

Polo-like kinases (PLKs) are conserved eukaryotic cell cycle regulators, which play multiple roles, particularly during mitosis. The function of Trypanosoma brucei PLK was investigated in procyclic and bloodstream-form parasites. In procyclic trypanosomes, RNA interference (RNAi) of PLK, or overexpression of TY1-epitope-tagged PLK (PLKty), but not overexpression of a kinase-dead variant, resulted in the accumulation of cells that had divided their nucleus but not their kinetoplast (2N1K cells). Analysis of basal bodies and flagella in these cells suggested the defect in kinetoplast division arose because of an inhibition of basal body duplication, which occurred when PLK expression levels were altered. Additionally, a defect in kDNA replication was observed in the 2N1K cells. However, the 2N1K cells obtained by each approach were not equivalent. Following PLK depletion, the single kinetoplast was predominantly located between the two divided nuclei, while in cells overexpressing PLKty, the kinetoplast was mainly found at the posterior end of the cell, suggesting a role for PLK kinase activity in basal body and kinetoplast migration. PLK RNAi in bloodstream trypanosomes also delayed kinetoplast division, and was further observed to inhibit furrow ingression during cytokinesis. Notably, no additional roles were detected for trypanosome PLK in mitosis, setting this protein kinase apart from its counterparts in other eukaryotes.

Indexed as

Trypanosoma brucei bruceiAnimalsCell Cycle ProteinsCell SeparationCytokinesisDNA, KinetoplastDNA ReplicationFlagellaPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsProtozoan ProteinsRNA InterferenceCell Cycle ProteinsDNA, KinetoplastPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsProtozoan Proteins

Identifiers

PMID17662039
PMCPMC2169650
OpenAlexW2164086894

What OpenQuestion holds

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LicenceCC BY
Read underepoch 390

Registered trials

None linked

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.