Evidence map›Paper›PMID 9182664›Full record

ArticleThe Journal of cell biology1997

Type II myosin heavy chain encoded by the myo2 gene composes the contractile ring during cytokinesis in Schizosaccharomyces pombe.

C Kitayama, A Sugimoto, M Yamamoto

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 100 papers.

0numbers the graph read from it
0cells of the map it votes in
100citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

100 citing papers in PubMed, 210 citations in OpenAlex.

  1. Article
  2. Article
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  4. Regulation of Yeast Cytokinesis by Calcium.Journal of fungi (Basel, Switzerland) · 2025
    Review
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  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Article
  12. Review
  13. Article
  14. Cleavage-furrow formation without F-actin inProceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  15. Review
  16. Review
  17. Article
  18. Molecular Mechanism of Cytokinesis.Annual review of biochemistry · 2019
    Review
  19. Article
  20. Article

40 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.

C KitayamaDepartment of Biophysics and Biochemistry, Graduate School of Science, University of Tokyo, Hongo, Tokyo 113, Japan.
A Sugimoto
M Yamamoto
Tokyo University of Science · JPThe University of Tokyo · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We cloned the myo2 gene of Schizosaccharomyces pombe, which encodes a type II myosin heavy chain, by virtue of its ability to promote diploidization in fission yeast cells. The myo2 gene encodes 1,526 amino acids in a single open reading frame. Myo2p shows homology to the head domains and the coiledcoil tail of the conventional type II myosin heavy chain and carries putative binding sites for ATP and actin. It also carries the IQ motif, which is a presumed binding site for the myosin light chain. However, Myo2p apparently carries only one IQ motif, while its counterparts in other species have two. There are nine proline residues, which should break alpha-helix, in the COOH-terminal coiled-coil region of Myo2p. Thus, Myo2p is rather unusual as a type II myosin heavy chain. Disruption of myo2 inhibited cell proliferation. myo2Delta cells showed normal punctate distribution of interphase actin, but they produced irregular actin rings and septa and were impaired in cell separation. Overproduction of Myo2p was also lethal, apparently blocking actin relocation. Nuclear division proceeded without actin ring formation and cytokinesis in cells overexpressing Myo2p, giving rise to multinucleated cells with dumbbell morphology. Analysis using tagged Myo2p revealed that Myo2p colocalizes with actin in the contractile ring, suggesting that Myo2p is a component of the ring and responsible for its contraction. Furthermore, genetic evidence suggested that the acto-myosin system may interact with the Ras pathway, which regulates mating and the maintenance of cell morphology in S. pombe.

Indexed as

Cell Cycle ProteinsMyosin Type IIMyosin Type VSaccharomyces cerevisiae ProteinsSchizosaccharomyces pombe ProteinsAmino Acid SequenceBacterial ProteinsCell DivisionCloning, MolecularFungal ProteinsGene DeletionGene ExpressionGenes, FungalHaploidyMolecular Sequence DataMyosin Heavy ChainsBacterial ProteinsCell Cycle ProteinsFungal ProteinsMYO2 protein, S cerevisiaeMYO2 protein, S pombeMyosin Heavy ChainsMyosinsMyosin Type IIMyosin Type VSaccharomyces cerevisiae Proteinsscd2 protein, S pombeSchizosaccharomyces pombe Proteins

Identifiers

PMID9182664
PMCPMC2132538
OpenAlexW2123685989

What OpenQuestion holds

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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.