Evidence map›Paper›PMID 9774337›Full record

ArticleThe EMBO journal1998

Gelsolin and functionally similar actin-binding proteins are regulated by lysophosphatidic acid.

K Meerschaert, V De Corte, Y De Ville, J Vandekerckhove, J Gettemans

Abstract read
In one paragraph

Article in The EMBO journal, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 29 papers.

0numbers the graph read from it
0cells of the map it votes in
29citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

29 citing papers in PubMed, 94 citations in OpenAlex.

  1. Article
  2. Review
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  4. Review
  5. Review
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. The protective effects of plasma gelsolin on stroke outcome in rats.Experimental & translational stroke medicine · 2011
    Article
  12. Article
  13. Plasma gelsolin modulates cellular response to sphingosine 1-phosphate.American journal of physiology. Cell physiology · 2010
    Article
  14. Aiming drug discovery at lysophosphatidic acid targets.British journal of pharmacology · 2010
    Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Article
  20. 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 1 institution in 1 country.

K MeerschaertFlanders Interuniversity Institute for Biotechnology (V.I.B.) and Department of Biochemistry, Faculty of Medicine, Universiteit Gent, Ledeganckstraat 35, B-9000 Gent, Belgium.
V De Corte
Y De Ville
J Vandekerckhove
J Gettemans
Vlaams Instituut voor Biotechnologie · BE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An extensive survey was carried out for compounds capable of regulating actin-binding proteins in a manner similar to phosphatidylinositol 4,5 bisphosphate (PI 4,5-P2). For this purpose we developed a sensitive assay involving release of radioactively phosphorylated actin from the fragminP-actin complex. We found that the structurally simplest lysophospholipid, lysophosphatidic acid (LPA), dissociated the complex between fragminP and actin, whereas other lysophospholipids or sphingosine-1-phosphate were inactive. Furthermore, LPA inhibited the F-actin severing activity of human gelsolin, purified from plasma or as recombinant protein, mouse adseverin and Physarum fragminP. Dissociation of actin-containing complexes by LPA analyzed by gelfiltration indicated that LPA is active as a monomer, in contrast to PI 4,5-P2. We further show that binding of LPA to these actin-regulatory proteins promotes their phosphorylation by pp60(c-src). A PI 4,5-P2-binding peptide counteracted the effects mediated by LPA, suggesting that LPA binds to the same target region in these actin-binding proteins. When both LPA and PI 4,5-P2 were used in combination we found that LPA reduced the threshold concentration at which PI 4,5-P2 was active. Significantly, LPA promoted the release of gelsolin from barbed actin filaments in octylglucoside-permeabilized human platelets. These results suggest that lysophosphatidic acid could act as an intracellular modulator of actin-binding proteins. Our findings can also explain agonist-induced changes in the actin cytoskeleton that are not mediated by polyphosphoinositides.

Indexed as

ActinsAmino Acid SequenceAnimalsEgtazic AcidGelsolinHumansLysophospholipidsMiceMicrofilament ProteinsMolecular Sequence DataPhosphatidylinositol 4,5-DiphosphatePhosphorylationProtein BindingActinsEgtazic AcidGelsolinLysophospholipidsMicrofilament ProteinsPhosphatidylinositol 4,5-Diphosphate

Identifiers

PMID9774337
PMCPMC1170920
OpenAlexW1981501419

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.