Evidence map›Paper›PMID 9950677›Full record

ArticleMolecular biology of the cell1999

The multiple roles of Cyk1p in the assembly and function of the actomyosin ring in budding yeast.

K B Shannon, R Li

Abstract read
In one paragraph

Article in Molecular biology of the cell, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 49 papers.

0numbers the graph read from it
0cells of the map it votes in
49citing papers in PubMed
–field-weighted citation impact
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

49 citing papers in PubMed.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Review
  8. Article
  9. Budding YeastG3 (Bethesda, Md.) · 2018
    Article
  10. Article
  11. Mechanics and regulation of cytokinesis in budding yeast.Seminars in cell & developmental biology · 2017
    Review
  12. Review
  13. Actomyosin ring driven cytokinesis in budding yeast.Seminars in cell & developmental biology · 2016
    Review
  14. Article
  15. Article
  16. Review
  17. Review
  18. Article
  19. Article
  20. Article
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

2 authors.

K B ShannonDepartment of Cell Biology, Harvard Medical School, Boston, Massachusetts 02115, USA.
R Li

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The budding yeast IQGAP-like protein Cyk1p/Iqg1p localizes to the mother-bud junction during anaphase and has been shown to be required for the completion of cytokinesis. In this study, video microscopy analysis of cells expressing green fluorescent protein-tagged Cyk1p/Iqg1p demonstrates that Cyk1p/Iqg1p is a dynamic component of the contractile ring during cytokinesis. Furthermore, in the absence of Cyk1p/Iqg1p, myosin II fails to undergo the contraction-like size change at the end of mitosis. To understand the mechanistic role of Cyk1p/Iqg1p in actomyosin ring assembly and dynamics, we have investigated the role of the structural domains that Cyk1p/Iqg1p shares with IQGAPs. An amino terminal portion containing the calponin homology domain binds to actin filaments and is required for the assembly of actin filaments to the ring. This result supports the hypothesis that Cyk1p/Iqg1p plays a direct role in F-actin recruitment. Deletion of the domain harboring the eight IQ motifs abolishes the localization of Cyk1p/Iqg1p to the bud neck, suggesting that Cyk1p/Iqg1p may be localized through interactions with a calmodulin-like protein. Interestingly, deletion of the COOH-terminal GTPase-activating protein-related domain does not affect Cyk1p/Iqg1p localization or actin recruitment to the ring but prevents actomyosin ring contraction. In vitro binding experiments show that Cyk1p/Iqg1p binds to calmodulin, Cmd1p, in a calcium-dependent manner, and to Tem1p, a small GTP-binding protein previously found to be required for the completion of anaphase. These results demonstrate the critical function of Cyk1p/Iqg1p in regulating various steps of actomyosin ring assembly and cytokinesis.

Indexed as

Monomeric GTP-Binding ProteinsSaccharomyces cerevisiae ProteinsActomyosinAnaphaseBase SequenceBinding SitesCalciumCalmodulinCell DivisionDNA PrimersFungal ProteinsGene ExpressionGreen Fluorescent ProteinsGTPase-Activating ProteinsGTP-Binding ProteinsLuminescent ProteinsActomyosinCalciumCalmodulinDNA PrimersFungal ProteinsGreen Fluorescent ProteinsGTPase-Activating ProteinsGTP-Binding ProteinsLuminescent ProteinsMonomeric GTP-Binding ProteinsProteinsras GTPase-Activating Proteinsras ProteinsRecombinant Fusion ProteinsSaccharomyces cerevisiae ProteinsTEM1 protein, S cerevisiae

Identifiers

PMID9950677
PMCPMC25169

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.