Evidence map›Paper›PMID 12654901›Full record

ArticleThe Journal of cell biology2003

Mid2p stabilizes septin rings during cytokinesis in fission yeast.

Ana Berlin, Anne Paoletti, Fred Chang

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 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing 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

69 citing papers in PubMed, 154 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
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  10. The Roles of Septins in Regulating Fission Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
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  13. Article
  14. Article
  15. Review
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  20. Article

9 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 2 countries.

Ana BerlinDepartment of Microbiology, Columbia University College of Physicians and Surgeons, New York, NY 10032, USA.
Anne Paoletti
Fred Chang
Columbia University · USBiologie cellulaire et Cancer · FR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Septins are filament-forming proteins with a conserved role in cytokinesis. In the fission yeast Schizosaccharomyces pombe, septin rings appear to be involved primarily in cell-cell separation, a late stage in cytokinesis. Here, we identified a protein Mid2p on the basis of its sequence similarity to S. pombe Mid1p, Saccharomyces cerevisiae Bud4p, and Candida albicans Int1p. Like septin mutants, mid2delta mutants had delays in cell-cell separation. mid2delta mutants were defective in septin organization but not contractile ring closure or septum formation. In wild-type cells, septins assembled first during mitosis in a single ring and during septation developed into double rings that did not contract. In mid2delta cells, septins initially assembled in a single ring but during septation appeared in the cleavage furrow, forming a washer or disc structure. FRAP studies showed that septins are stable in wild-type cells but exchange 30-fold more rapidly in mid2delta cells. Mid2p colocalized with septins and required septins for its localization. A COOH-terminal pleckstrin homology domain of Mid2p was required for its localization and function. No genetic interactions were found between mid2 and the related gene mid1. Thus, these studies identify a new factor responsible for the proper stability and function of septins during cytokinesis.

Indexed as

Amino Acid SequenceBiomarkersCalcium-Binding ProteinsCell Cycle ProteinsCell DivisionFungal ProteinsGreen Fluorescent ProteinsIntracellular Signaling Peptides and ProteinsLuminescent ProteinsMembrane GlycoproteinsMembrane ProteinsModels, BiologicalMolecular Sequence DataMutationProtein Structure, TertiaryRecombinant Fusion ProteinsBiomarkersCalcium-Binding ProteinsCell Cycle ProteinsFungal ProteinsGreen Fluorescent ProteinsIntracellular Signaling Peptides and ProteinsLuminescent ProteinsMembrane GlycoproteinsMembrane ProteinsMID2 protein, S cerevisiaeRecombinant Fusion ProteinsSaccharomyces cerevisiae Proteins

Identifiers

PMID12654901
PMCPMC2172768
OpenAlexW2160121928

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.