Evidence map›Paper›PMID 15987738›Full record

ArticleMolecular biology of the cell2005

Multiple myosin II heavy chain kinases: roles in filament assembly control and proper cytokinesis in Dictyostelium.

Shigehiko Yumura, Masashi Yoshida, Venkaiah Betapudi, Lucila S Licate, Yoshiaki Iwadate, Akira Nagasaki, Taro Q P Uyeda, Thomas T Egelhoff

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 54 papers.

0numbers the graph read from it
0cells of the map it votes in
54citing papers in PubMed
2.0field-weighted citation impact, top 15% 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

54 citing papers in PubMed, 87 citations in OpenAlex.

  1. Article
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  10. Article
  11. Article
  12. Article
  13. Cytokinesis: Robust cell shape regulation.Seminars in cell & developmental biology · 2016
    Review
  14. Article
  15. Cell shape regulation through mechanosensory feedback control.Journal of the Royal Society, Interface · 2015
    Article
  16. Pharmacological activation of myosin II paralogs to correct cell mechanics defects.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  17. Article
  18. Article
  19. Article
  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

8 authors at 3 institutions in 2 countries.

Shigehiko YumuraDepartment of Biology, Faculty of Science, Yamaguchi University, Yamaguchi 753-8512, Japan.
Masashi Yoshida
Venkaiah Betapudi
Lucila S Licate
Yoshiaki Iwadate
Akira Nagasaki
Taro Q P Uyeda
Thomas T Egelhoff
Case Western Reserve University · USYamaguchi University · JPNational Institute of Advanced Industrial Science and Technology · JP

Funding

Myosin Assembly in DictyosteliumR01GM050009 · NIGMS · CLEVELAND CLINIC LERNER COM-CWRU · PI EGELHOFF, THOMAS · 1998 to 2017
$4.7M
CELLULAR APPROACHES TO MYOSIN REGULATIONR29GM050009 · NIGMS · CASE WESTERN RESERVE UNIVERSITY · PI EGELHOFF, THOMAS T · 1993 to 1997
–
NIGMS NIH HHS GM50009NIGMS NIH HHS R01 GM050009
6 · The paper itself

Abstract

Myosin II filament assembly in Dictyostelium discoideum is regulated via phosphorylation of residues located in the carboxyl-terminal portion of the myosin II heavy chain (MHC) tail. A series of novel protein kinases in this system are capable of phosphorylating these residues in vitro, driving filament disassembly. Previous studies have demonstrated that at least three of these kinases (MHCK A, MHCK B, and MHCK C) display differential localization patterns in living cells. We have created a collection of single, double, and triple gene knockout cell lines for this family of kinases. Analysis of these lines reveals that three MHC kinases appear to represent the majority of cellular activity capable of driving myosin II filament disassembly, and reveals that cytokinesis defects increase with the number of kinases disrupted. Using biochemical fractionation of cytoskeletons and in vivo measurements via fluorescence recovery after photobleaching (FRAP), we find that myosin II overassembly increases incrementally in the mutants, with the MHCK A(-)/B(-)/C(-) triple mutant showing severe myosin II overassembly. These studies suggest that the full complement of MHC kinases that significantly contribute to growth phase and cytokinesis myosin II disassembly in this organism has now been identified.

Indexed as

AnimalsCalcium-Calmodulin-Dependent Protein KinasesCell LineCytokinesisCytoskeletonDictyosteliumGenes, ReporterMyosin Heavy ChainsMyosin Type IIPhosphorylationProtein Processing, Post-TranslationalProtozoan ProteinsRecombinant Fusion ProteinsCalcium-Calmodulin-Dependent Protein Kinasesmyosin-heavy-chain kinaseMyosin Heavy ChainsMyosin Type IIProtozoan ProteinsRecombinant Fusion Proteins

Identifiers

PMID15987738
PMCPMC1196335
OpenAlexW2097648001

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.