Evidence map›Paper›PMID 12668659›Full record

ArticleThe Journal of cell biology2003

An anillin homologue, Mid2p, acts during fission yeast cytokinesis to organize the septin ring and promote cell separation.

Joseph J Tasto, Jennifer L Morrell, Kathleen L Gould

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 2003. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 81 papers.

0numbers the graph read from it
0cells of the map it votes in
81citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

81 citing papers in PubMed, 160 citations in OpenAlex.

  1. Article
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  5. Localization and function of septins are susceptible to epitope tagging.bioRxiv : the preprint server for biology · 2025
    Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Article
  11. The Roles of Septins in Regulating Fission Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Review
  20. Article

21 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

3 authors at 2 institutions in 1 country.

Joseph J TastoDepartment of Cell and Developmental Biology, Vanderbilt University School of Medicine, Nashville, TN 37232, USA.
Jennifer L Morrell
Kathleen L Gould
Howard Hughes Medical Institute · USVanderbilt University · US

Funding

TRAINING PROGRAM IN CELLULAR, BIOCHEMICAL, &MOLECULAR ST32GM008554 · NIGMS · VANDERBILT UNIVERSITY · PI PATTON, JAMES G. · 1995 to 2020
$7.4M
NIGMS NIH HHS T32 GM008554NIGMS NIH HHS T32GM08554
6 · The paper itself

Abstract

Anillin is a conserved protein required for cell division (Field, C.M., and B.M. Alberts. 1995. J. Cell Biol. 131:165-178; Oegema, K., M.S. Savoian, T.J. Mitchison, and C.M. Field. 2000. J. Cell Biol. 150:539-552). One fission yeast homologue of anillin, Mid1p, is necessary for the proper placement of the division site within the cell (Chang, F., A. Woollard, and P. Nurse. 1996. J. Cell Sci. 109(Pt 1):131-142; Sohrmann, M., C. Fankhauser, C. Brodbeck, and V. Simanis. 1996. Genes Dev. 10:2707-2719). Here, we identify and characterize a second fission yeast anillin homologue, Mid2p, which is not orthologous with Mid1p. Mid2p localizes as a single ring in the middle of the cell after anaphase in a septin- and actin-dependent manner and splits into two rings during septation. Mid2p colocalizes with septins, and mid2 Delta cells display disorganized, diffuse septin rings and a cell separation defect similar to septin deletion strains. mid2 gene expression and protein levels fluctuate during the cell cycle in a sep1- and Skp1/Cdc53/F-box (SCF)-dependent manner, respectively, implying that Mid2p activity must be carefully regulated. Overproduction of Mid2p depolarizes cell growth and affects the organization of both the septin and actin cytoskeletons. In the presence of a nondegradable Mid2p fragment, the septin ring is stabilized and cell cycle progression is delayed. These results suggest that Mid2p influences septin ring organization at the site of cell division and its turnover might normally be required to permit septin ring disassembly.

Indexed as

Contractile ProteinsActinsAmino Acid SequenceCalcium-Binding ProteinsCell DivisionCyclin-Dependent KinasesDNA-Binding ProteinsFungal ProteinsGene DeletionGene Expression Regulation, FungalGenes, FungalGreen Fluorescent ProteinsHumansIntracellular Signaling Peptides and ProteinsLuminescent ProteinsMembrane GlycoproteinsActinsanillinCalcium-Binding ProteinsContractile ProteinsCyclin-Dependent KinasesDNA-Binding ProteinsFungal ProteinsGreen Fluorescent ProteinsIntracellular Signaling Peptides and ProteinsLuminescent ProteinsMembrane GlycoproteinsMembrane ProteinsMID2 protein, S cerevisiaeRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsSFP1 protein, S cerevisiae

Identifiers

PMID12668659
PMCPMC2172762
OpenAlexW2129932376

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.