Evidence map›Paper›PMID 12181339›Full record

ArticleMolecular biology of the cell2002

Dual regulation of actin rearrangement through lysophosphatidic acid receptor in neuroblast cell lines: actin depolymerization by Ca(2+)-alpha-actinin and polymerization by rho.

Nobuyuki Fukushima, Isao Ishii, Yoshiaki Habara, Cara B Allen, Jerold Chun

Open access · greenAbstract read
In one paragraph

Article in Molecular biology of the cell, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.

0numbers the graph read from it
0cells of the map it votes in
24citing papers in PubMed
1.6field-weighted citation impact, top 17% 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

24 citing papers in PubMed, 62 citations in OpenAlex.

  1. Review
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  11. Autotaxin⁻Lysophosphatidic Acid Signaling in Alzheimer's Disease.International journal of molecular sciences · 2018
    Review
  12. Article
  13. Review
  14. Review
  15. Article
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  18. Article
  19. ERM proteins regulate growth cone responses to Sema3A.The Journal of comparative neurology · 2008
    Article
  20. Intermediate filament protein synemin contributes to the migratory properties of astrocytoma cells by influencing the dynamics of the actin cytoskeleton.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2008
    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

5 authors at 3 institutions in 2 countries.

Nobuyuki FukushimaDepartment of Molecular Biochemistry, Hokkaido University Graduate School of Medicine, Sapporo 060-8638, Japan. nfuku@med.hokudai.ac.jp
Isao Ishii
Yoshiaki Habara
Cara B Allen
Jerold Chun
Hokkaido University · JPMerck & Co., Inc., Rahway, NJ, USA (United States) · USNeurosciences Institute · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysophosphatidic acid (LPA) is a potent lipid mediator with actions on many cell types. Morphological changes involving actin polymerization are mediated by at least two cognate G protein-coupled receptors, LPA(1)/EDG-2 or LPA(2)/EDG-4. Herein, we show that LPA can also induce actin depolymerization preceding actin polymerization within single TR mouse immortalized neuroblasts. Actin depolymerization resulted in immediate loss of membrane ruffling, whereas actin polymerization resulted in process retraction. Each pathway was found to be independent: depolymerization mediated by intracellular calcium mobilization, and alpha-actinin activity and polymerization mediated by the activation of the small Rho GTPase. alpha-Actinin-mediated depolymerization seems to be involved in growth cone collapse of primary neurons, indicating a physiological significance of LPA-induced actin depolymerization. Further evidence for dual regulation of actin rearrangement was found by heterologous retroviral transduction of either lpa(1) or lpa(2) in B103 cells that neither express LPA receptors nor respond to LPA, to confer both forms of LPA-induced actin rearrangements. These results suggest that diverging intracellular signals from a single type of LPA receptor could regulate actin depolymerization, as well as polymerization, within a single cell. This dual actin rearrangement may play a novel, important role in regulation of the neuronal morphology and motility during brain development.

Indexed as

Receptors, G-Protein-CoupledActininActinsAmidesAnimalsCalciumCell MembraneCells, CulturedCell SizeChelating AgentsCytoskeletonEgtazic AcidEnzyme ActivationEnzyme InhibitorsImmunohistochemistryLysophospholipids1,2-bis(2-aminophenoxy)ethane N,N,N',N'-tetraacetic acid acetoxymethyl esterActininActinsAmidesCalciumChelating AgentsEgtazic AcidEnzyme InhibitorsLysophospholipidsPyridinesReceptors, Cell SurfaceReceptors, G-Protein-CoupledReceptors, Lysophosphatidic Acidrho GTP-Binding ProteinsType C PhospholipasesY 27632

Identifiers

PMID12181339
PMCPMC117935
OpenAlexW2136546959

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.