Evidence map›Paper›PMID 17509155›Full record

ArticleBMC cell biology2007

Phospholipase C and myosin light chain kinase inhibition define a common step in actin regulation during cytokinesis.

Raymond Wong, Lacramioara Fabian, Arthur Forer, Julie A Brill

Open access · goldAbstract read
In one paragraph

Article in BMC cell biology, 2007. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
2.1field-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

27 citing papers in PubMed, 66 citations in OpenAlex.

  1. Article
  2. PLCβ2 Promotes VEGF-Induced Vascular Permeability.Arteriosclerosis, thrombosis, and vascular biology · 2022
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  3. Group BPathogens (Basel, Switzerland) · 2022
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  7. Endoplasmic reticulum (ER) CaThe Journal of biological chemistry · 2017
    Article
  8. nsPEF-induced PIPBiochemistry and biophysics reports · 2017
    Article
  9. Article
  10. Review
  11. Article
  12. Calcium waves occur as Drosophila oocytes activate.Proceedings of the National Academy of Sciences of the United States of America · 2015
    Article
  13. Review
  14. Article
  15. Article
  16. Article
  17. Article
  18. Article
  19. Article
  20. Myosin light chain kinases and phosphatase in mitosis and cytokinesis.Archives of biochemistry and biophysics · 2011
    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 3 institutions in 1 country.

Raymond WongProgram in Developmental and Stem Cell Biology, The Hospital for Sick Children, TMDT Building, East Tower, Toronto, Ontario, Canada. re.wong@utoronto.ca <re.wong@utoronto.ca>
Lacramioara Fabian
Arthur Forer
Julie A Brill
Hospital for Sick Children · CAUniversity of Toronto · CAYork University · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

backgroundPhosphatidylinositol 4,5-bisphosphate (PIP2) is required for successful completion of cytokinesis. In addition, both PIP2 and phosphoinositide-specific phospholipase C (PLC) have been localized to the cleavage furrow of dividing mammalian cells. PLC hydrolyzes PIP2 to yield diacylglycerol (DAG) and inositol trisphosphate (IP3), which in turn induces calcium (Ca2+) release from the ER. Several studies suggest PIP2 must be hydrolyzed continuously for continued cleavage furrow ingression. The majority of these studies employ the N-substituted maleimide U73122 as an inhibitor of PLC. However, the specificity of U73122 is unclear, as its active group closely resembles the non-specific alkylating agent N-ethylmaleimide (NEM). In addition, the pathway by which PIP2 regulates cytokinesis remains to be elucidated.

resultsHere we compared the effects of U73122 and the structurally unrelated PLC inhibitor ET-18-OCH3 (edelfosine) on cytokinesis in crane-fly and Drosophila spermatocytes. Our data show that the effects of U73122 are indeed via PLC because U73122 and ET-18-OCH3 produced similar effects on cell morphology and actin cytoskeleton organization that were distinct from those caused by NEM. Furthermore, treatment with the myosin light chain kinase (MLCK) inhibitor ML-7 caused cleavage furrow regression and loss of both F-actin and phosphorylated myosin regulatory light chain from the contractile ring in a manner similar to treatment with U73122 and ET-18-OCH3.

conclusionWe have used multiple inhibitors to examine the roles of PLC and MLCK, a predicted downstream target of PLC regulation, in cytokinesis. Our results are consistent with a model in which PIP2 hydrolysis acts via Ca2+ to activate myosin via MLCK and thereby control actin dynamics during constriction of the contractile ring.

Indexed as

CytokinesisActinsAlkylationAnimalsAzepinesCattleDrosophila melanogasterEnzyme ActivationEnzyme InhibitorsEstrenesEthylmaleimideMaleMyosin-Light-Chain KinaseMyosin Light ChainsNaphthalenesPhospholipid Ethers1-(6-((3-methoxyestra-1,3,5(10)-trien-17-yl)amino)hexyl)-1H-pyrrole-2,5-dioneActinsAzepinesedelfosineEnzyme InhibitorsEstrenesEthylmaleimideML 7Myosin-Light-Chain KinaseMyosin Light ChainsNaphthalenesPhospholipid EthersPyrrolidinonesType C Phospholipases

Identifiers

PMID17509155
PMCPMC1888687
OpenAlexW2007125318

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.