Evidence map›Paper›PMID 19109423›Full record

ArticleMolecular biology of the cell2009

The anaphase-promoting complex promotes actomyosin-ring disassembly during cytokinesis in yeast.

Gregory H Tully, Ryuichi Nishihama, John R Pringle, David O Morgan

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 28 papers.

0numbers the graph read from it
0cells of the map it votes in
28citing papers in PubMed
1.1field-weighted citation impact, top 25% 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

28 citing papers in PubMed, 38 citations in OpenAlex.

  1. Review
  2. Septin Organization and Dynamics for Budding Yeast Cytokinesis.Journal of fungi (Basel, Switzerland) · 2024
    Review
  3. Article
  4. Molecular Mechanism of Cytokinesis.Annual review of biochemistry · 2019
    Review
  5. Article
  6. Mechanics and regulation of cytokinesis in budding yeast.Seminars in cell & developmental biology · 2017
    Review
  7. Article
  8. Review
  9. Actomyosin ring driven cytokinesis in budding yeast.Seminars in cell & developmental biology · 2016
    Review
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Article
  17. Article
  18. Review
  19. Cell cycle regulation of Rho signaling pathways.Cell cycle (Georgetown, Tex.) · 2012
    Review
  20. Review
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

4 authors at 2 institutions in 1 country.

Gregory H TullyDepartment of Physiology, University of California, San Francisco, CA 94158, USA.
Ryuichi Nishihama
John R Pringle
David O Morgan
Stanford University · USUniversity of California, San Francisco · US

Funding

MORPHOGENESIS AND CYTOKINESIS IN THE YEAST CELL CYCLER37GM031006 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI PRINGLE, JOHN R · 2000 to 2010
$4.8M
MOLECULAR CONTROL OF CELL PROLIFERATIONR01GM053270 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MORGAN, DAVID OWEN · 1995 to 2010
$4.2M
Molecular Control of Cell ProliferationR37GM053270 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI MORGAN, DAVID OWEN · 2011 to 2015
$1.8M
GENETIC STUDY OF THE YEAST CELL CYCLER01GM031006 · NIGMS · UNIVERSITY OF NORTH CAROLINA CHAPEL HILL · PI PRINGLE, JOHN R · 1986 to 1999
–
NIGMS NIH HHS GM31006NIGMS NIH HHS GM53270NIGMS NIH HHS R01 GM031006NIGMS NIH HHS R01 GM053270NIGMS NIH HHS R37 GM031006NIGMS NIH HHS R37 GM053270
6 · The paper itself

Abstract

The anaphase-promoting complex (APC) is a ubiquitin ligase that controls progression through mitosis by targeting specific proteins for degradation. It is unclear whether the APC also contributes to the control of cytokinesis, the process that divides the cell after mitosis. We addressed this question in the yeast Saccharomyces cerevisiae by studying the effects of APC mutations on the actomyosin ring, a structure containing actin, myosin, and several other proteins that forms at the division site and is important for cytokinesis. In wild-type cells, actomyosin-ring constituents are removed progressively from the ring during contraction and disassembled completely thereafter. In cells lacking the APC activator Cdh1, the actomyosin ring contracts at a normal rate, but ring constituents are not disassembled normally during or after contraction. After cytokinesis in mutant cells, aggregates of ring proteins remain at the division site and at additional foci in other parts of the cell. A key target of APC(Cdh1) is the ring component Iqg1, the destruction of which contributes to actomyosin-ring disassembly. Deletion of CDH1 also exacerbates actomyosin-ring disassembly defects in cells with mutations in the myosin light-chain Mlc2, suggesting that Mlc2 and the APC employ independent mechanisms to promote ring disassembly during cytokinesis.

Indexed as

CytokinesisActomyosinAnaphase-Promoting Complex-CyclosomeMutationMyosin Light ChainsProtein TransportSaccharomyces cerevisiaeSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase ComplexesActomyosinAnaphase-Promoting Complex-CyclosomeMyosin Light ChainsSaccharomyces cerevisiae ProteinsUbiquitin-Protein Ligase Complexes

Identifiers

PMID19109423
PMCPMC2642741
OpenAlexW2139047645

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.