Evidence map›Paper›PMID 18694934›Full record

ArticleThe Journal of biological chemistry2008

Phosphorylation of MyoGEF on Thr-574 by Plk1 promotes MyoGEF localization to the central spindle.

Michael Asiedu, Di Wu, Fumio Matsumura, Qize Wei

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 papers.

0numbers the graph read from it
0cells of the map it votes in
19citing papers in PubMed
1.5field-weighted citation impact, top 20% 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

19 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Human phosphatase CDC14A is recruited to the cell leading edge to regulate cell migration and adhesion.Proceedings of the National Academy of Sciences of the United States of America · 2016
    Article
  6. Article
  7. Article
  8. Review
  9. Article
  10. Review
  11. Cell cycle regulation of Rho signaling pathways.Cell cycle (Georgetown, Tex.) · 2012
    Review
  12. Myosin light chain kinases and phosphatase in mitosis and cytokinesis.Archives of biochemistry and biophysics · 2011
    Review
  13. Review
  14. Article
  15. Polo-box domain: a versatile mediator of polo-like kinase function.Cellular and molecular life sciences : CMLS · 2010
    Review
  16. Mechanics of cytokinesis in eukaryotes.Current opinion in cell biology · 2010
    Review
  17. Article
  18. Article
  19. 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

4 authors at 2 institutions in 1 country.

Michael AsieduDepartment of Biochemistry, Kansas State University, Manhattan, Kansas 66506, USA.
Di Wu
Fumio Matsumura
Qize Wei
Kansas State University · USRutgers, The State University of New Jersey · US

Funding

WEIGHT CONTROL, CELL SIGNALING AND CANCER PREVENTIONP20RR015563 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI ZUFFEREY, RACHEL · 2000 to 2009
$20.1M
TRAFFICKING OF THE PLASMA MEMBRANE CA2+-ATPASE TO RAFTSP20RR017708 · NCRR · UNIVERSITY OF KANSAS LAWRENCE · PI FISCHER, CHRISTOPHER JAMES · 2002 to 2011
$20.1M
Identification of downstream signals for Pitx2aK22HL071542 · NHLBI · KANSAS STATE UNIVERSITY · PI WEI, QIZE · 2005 to 2006
$357k
NCRR NIH HHS P20 RR017708NCRR NIH HHS P20 RR15563NCRR NIH HHS P20 RR17708NHLBI NIH HHS K22 HL071542
6 · The paper itself

Abstract

We reported previously that a guanine nucleotide exchange factor, MyoGEF, localizes to the central spindle, activates RhoA, and is required for cytokinesis. In this study, we have found that Plk1 (polo-like kinase 1) can phosphorylate MyoGEF, thereby recruiting MyoGEF to the central spindle as well as enhancing MyoGEF activity toward RhoA. The in vitro kinase assay shows that Plk1 can phosphorylate MyoGEF on threonine 574. Immunoprecipitation/immunoblot analysis demonstrates that mutation of threonine 574 to alanine dramatically decreases threonine phosphorylation of MyoGEF in transfected HeLa cells, suggesting that threonine 574 is phosphorylated in vivo. Consistent with these observations, immunofluorescence shows that Plk1 and MyoGEF colocalize at the spindle pole and central spindle during mitosis and cytokinesis. Importantly, RNA interference-mediated depletion of Plk1 interferes with the localization of MyoGEF at the spindle pole and central spindle. Moreover, mutation of threonine 574 to alanine in MyoGEF or depletion of Plk1 by RNA interference leads to a decrease in MyoGEF activity toward RhoA in HeLa cells. Therefore, our results suggest that Plk1 can regulate MyoGEF activity and localization, contributing to the regulation of cytokinesis.

Indexed as

Spindle ApparatusAlanineCell CycleCell Cycle ProteinsCytokinesisGuanine Nucleotide Exchange FactorsHeLa CellsHumansMicroscopy, FluorescenceMitosisModels, BiologicalPhosphorylationPlasmidsPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsAlanineCell Cycle ProteinsGuanine Nucleotide Exchange FactorsPLEKHG6 protein, humanPolo-Like Kinase 1Protein Serine-Threonine KinasesProto-Oncogene ProteinsRNAThreonine

Identifiers

PMID18694934
PMCPMC2568926
OpenAlexW2061725521

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.