Evidence map›Paper›PMID 15353548›Full record

ArticleThe Journal of cell biology2004

Phosphorylation of actopaxin regulates cell spreading and migration.

Dominic M Clarke, Michael C Brown, David P LaLonde, Christopher E Turner

Open access · bronzeAbstract readComparative Study
In one paragraph

Article in The Journal of cell biology, 2004. 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
1.5field-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

24 citing papers in PubMed, 52 citations in OpenAlex.

  1. Article
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  14. LNK (SH2B3) is a key regulator of integrin signaling in endothelial cells and targets α-parvin to control cell adhesion and migration.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2012
    Article
  15. Stages of ciliogenesis and regulation of ciliary length.Differentiation; research in biological diversity · 2012
    Review
  16. Article
  17. Article
  18. Article
  19. Article
  20. Paxillin comes of age.Journal of cell science · 2008
    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.

Dominic M ClarkeDepartment of Cell Biology and Developmental Biology, State University of New York Upstate Medical University, Syracuse, NY 13210, USA.
Michael C Brown
David P LaLonde
Christopher E Turner
SUNY Upstate Medical University · US

Funding

ILK-Actopaxin Interactions in Cell SignalingR01HL070244 · NHLBI · UPSTATE MEDICAL UNIVERSITY · PI TURNER, CHRISTOPHER E · 2002 to 2010
$3.0M
NHLBI NIH HHS R01 HL070244
6 · The paper itself

Abstract

Actopaxin is an actin and paxillin binding protein that localizes to focal adhesions. It regulates cell spreading and is phosphorylated during mitosis. Herein, we identify a role for actopaxin phosphorylation in cell spreading and migration. Stable clones of U2OS cells expressing actopaxin wild-type (WT), nonphosphorylatable, and phosphomimetic mutants were developed to evaluate actopaxin function. All proteins targeted to focal adhesions, however the nonphosphorylatable mutant inhibited spreading whereas the phosphomimetic mutant cells spread more efficiently than WT cells. Endogenous and WT actopaxin, but not the nonphosphorylatable mutant, were phosphorylated in vivo during cell adhesion/spreading. Expression of the nonphosphorylatable actopaxin mutant significantly reduced cell migration, whereas expression of the phosphomimetic increased cell migration in scrape wound and Boyden chamber migration assays. In vitro kinase assays demonstrate that extracellular signal-regulated protein kinase phosphorylates actopaxin, and treatment of U2OS cells with the MEK1 inhibitor UO126 inhibited adhesion-induced phosphorylation of actopaxin and also inhibited cell migration.

Indexed as

ActininAmino Acid SequenceButadienesCalponinsCell Line, TumorCell MovementCell SizeClone CellsEnzyme InhibitorsFocal AdhesionsHumansKineticsMicrofilament ProteinsMutationNitrilesPhosphorylationActininButadienesCalponinsEnzyme InhibitorsMicrofilament ProteinsNitrilesPARVA protein, humanU 0126

Identifiers

PMID15353548
PMCPMC2172128
OpenAlexW2035191988

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.