Evidence map›Paper›PMID 14665465›Full record

ArticleEukaryotic cell2003

Two Dictyostelium orthologs of the prokaryotic cell division protein FtsZ localize to mitochondria and are required for the maintenance of normal mitochondrial morphology.

Paul R Gilson, Xuan-Chuan Yu, Dale Hereld, Christian Barth, Amelia Savage, Ben R Kiefel, Sui Lay, Paul R Fisher, William Margolin, Peter L Beech

Open access · diamondAbstract readComparative Study
In one paragraph

Article in Eukaryotic cell, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
1.7field-weighted citation impact, top 16% 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

31 citing papers in PubMed, 69 citations in OpenAlex.

  1. Inhibition of mitochondrial dynamics inFrontiers in cell and developmental biology · 2026
    Article
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  4. Enhanced chloroplast FtsZ-ring constriction by the ARC6-ARC3 module inProceedings of the National Academy of Sciences of the United States of America · 2025
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  6. Review
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  14. Review
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  16. An ancestral bacterial division system is widespread in eukaryotic mitochondria.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Mechanisms of mitochondrial fission and fusion.Cold Spring Harbor perspectives in biology · 2013
    Review
  18. Article
  19. Article
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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

10 authors at 3 institutions in 2 countries.

Paul R GilsonCentre for Cellular and Molecular Biology, School of Biological and Chemical Sciences, Deakin University, Victoria 3125, Australia. gilson@wehi.edu.au
Xuan-Chuan Yu
Dale Hereld
Christian Barth
Amelia Savage
Ben R Kiefel
Sui Lay
Paul R Fisher
William Margolin
Peter L Beech
La Trobe University · AUCentre for Cellular and Molecular Biology · INDeakin University · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

In bacteria, the protein FtsZ is the principal component of a ring that constricts the cell at division. Though all mitochondria probably arose through a single, ancient bacterial endosymbiosis, the mitochondria of only certain protists appear to have retained FtsZ, and the protein is absent from the mitochondria of fungi, animals, and higher plants. We have investigated the role that FtsZ plays in mitochondrial division in the genetically tractable protist Dictyostelium discoideum, which has two nuclearly encoded FtsZs, FszA and FszB, that are targeted to the inside of mitochondria. In most wild-type amoebae, the mitochondria are spherical or rod-shaped, but in fsz-null mutants they become elongated into tubules, indicating that a decrease in mitochondrial division has occurred. In support of this role in organelle division, antibodies to FszA and FszA-green fluorescent protein (GFP) show belts and puncta at multiple places along the mitochondria, which may define future or recent sites of division. FszB-GFP, in contrast, locates to an electron-dense, submitochondrial body usually located at one end of the organelle, but how it functions during division is unclear. This is the first demonstration of two differentially localized FtsZs within the one organelle, and it points to a divergence in the roles of these two proteins.

Indexed as

Prokaryotic CellsAmino Acid MotifsAmino Acid SequenceAnimalsBacterial ProteinsBase PairingCell DivisionCytoskeletal ProteinsDatabases, FactualDictyosteliumDNA, ProtozoanFluorescent DyesGenes, ProtozoanMicroscopy, ImmunoelectronMitochondriaMolecular Sequence DataBacterial ProteinsCytoskeletal ProteinsDNA, ProtozoanFluorescent DyesFtsZ protein, BacteriaOrganic Chemicalsred dye CMXRos

Identifiers

PMID14665465
PMCPMC326642
OpenAlexW2130426932

What OpenQuestion holds

Textmetadata
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.