Evidence map›Paper›PMID 19808673›Full record

ArticleThe Journal of biological chemistry2009

Differential effects of lysophosphatidic acid and phosphatidylinositol 4,5-bisphosphate on actin dynamics by direct association with the actin-binding protein villin.

Alok Tomar, Sudeep P George, Sijo Mathew, Seema Khurana

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.

0numbers the graph read from it
0cells of the map it votes in
11citing papers in PubMed
0.8field-weighted citation impact, top 29% 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

11 citing papers in PubMed, 20 citations in OpenAlex.

  1. Article
  2. Review
  3. Article
  4. Article
  5. Article
  6. Article
  7. Phosphatidylinositol 4,5-bisphosphate regulates CapZβ1 and actin dynamics in response to mechanical strain.American journal of physiology. Heart and circulatory physiology · 2013
    Article
  8. Article
  9. Article
  10. Endocannabinoids and diacylglycerol kinase activity.Biochimica et biophysica acta · 2011
    Article
  11. Aiming drug discovery at lysophosphatidic acid targets.British journal of pharmacology · 2010
    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 1 institution in 1 country.

Alok TomarDepartment of Physiology, University of Tennessee Health Science Center, Memphis, Tennessee 38163, USA.
Sudeep P George
Sijo Mathew
Seema Khurana
University of Tennessee Health Science Center · US

Funding

ROLE OF VILLIN IN EPITHELIAL CELL SIGNAL TRANSDUCTIONR01DK054755 · NIDDK · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI KHURANA, SEEMA · 2000 to 2009
$3.1M
Regulation of epithelial cell motility by villin.R01DK065006 · NIDDK · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI KHURANA, SEEMA · 2004 to 2008
$1.6M
Regulation of epithelial cell homeostasis by actin microfilamentsR01DK081408 · NIDDK · UNIVERSITY OF TENNESSEE HEALTH SCI CTR · PI KHURANA, SEEMA · 2009 to 2010
$785k
NIDDK NIH HHS DK-54755NIDDK NIH HHS DK-65006NIDDK NIH HHS DK-81408NIDDK NIH HHS R01 DK054755NIDDK NIH HHS R01 DK065006NIDDK NIH HHS R01 DK081408
6 · The paper itself

Abstract

We have previously reported that the epithelial cell-specific actin-binding protein villin directly associates with phosphatidylinositol 4,5-bisphosphate (PIP(2)) through three binding sites that overlap with actin-binding sites in villin. As a result, association of villin with PIP(2) inhibits actin depolymerization and enhances actin cross-linking by villin. In this study, we demonstrate that these three PIP(2)-binding sites also bind the more hydrophilic phospholipid, lysophosphatidic acid (LPA) but with a higher affinity than PIP(2) (dissociation constant (K(d)) of 22 mum versus 39.5 mum for PIP(2)). More interestingly, unlike PIP(2), the association of villin with LPA inhibits all actin regulatory functions of villin. In addition, unlike PIP(2), LPA dramatically stimulates the tyrosine phosphorylation of villin by c-Src kinase. These studies suggest that in cells, selective interaction of villin with either PIP(2) or LPA could have dramatically different outcomes on actin reorganization as well as phospholipid-regulated cell signaling. These studies provide a novel regulatory mechanism for phospholipid-induced changes in the microfilament structure and cell function and suggest that LPA could be an intracellular regulator of the actin cytoskeleton.

Indexed as

Actin CytoskeletonActinsBinding SitesCSK Tyrosine-Protein KinaseHumansHydrophobic and Hydrophilic InteractionsLysophospholipidsMicrofilament ProteinsPhosphatidylinositol 4,5-DiphosphatePhosphorylationProtein BindingProtein-Tyrosine KinasesProto-Oncogene ProteinsSignal Transductionsrc-Family KinasesActinsCSK protein, humanCSK Tyrosine-Protein Kinaselysophosphatidic acidLysophospholipidsMicrofilament ProteinsPhosphatidylinositol 4,5-DiphosphateProtein-Tyrosine KinasesProto-Oncogene Proteinssrc-Family Kinasesvillin

Identifiers

PMID19808673
PMCPMC2790956
OpenAlexW1965676885

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.