Evidence map›Paper›PMID 10922062›Full record

ArticleProceedings of the National Academy of Sciences of the United States of America2000

Paxillin alpha and Crk-associated substrate exert opposing effects on cell migration and contact inhibition of growth through tyrosine phosphorylation.

H Yano, H Uchida, T Iwasaki, M Mukai, H Akedo, K Nakamura, S Hashimoto, H Sabe

Open access · greenAbstract read
In one paragraph

Article in Proceedings of the National Academy of Sciences of the United States of America, 2000. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
3.8field-weighted citation impact, top 6% 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

46 citing papers in PubMed, 89 citations in OpenAlex.

  1. Review
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  7. Endothelial cells promote metastasis of prostate cancer by enhancing autophagy.Journal of experimental & clinical cancer research : CR · 2018
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  18. Physiologic properties and regulation of the actin cytoskeleton in vascular smooth muscle.Journal of cardiovascular pharmacology and therapeutics · 2008
    Review
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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

8 authors at 3 institutions in 1 country.

H YanoDepartment of Molecular Biology, Osaka Bioscience Institute, Suita, Osaka 565-0874, Japan.
H Uchida
T Iwasaki
M Mukai
H Akedo
K Nakamura
S Hashimoto
H Sabe
Kyoto University · JPHyogo Medical University · JPOsaka Medical Center for Cancer and Cardiovascular Diseases · JP

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Protein tyrosine phosphorylation accompanies and is essential for integrin signaling. We have shown that tyrosine phosphorylation of paxillin alpha and Crk-associated substrate (p130(Cas)) is a prominent event on integrin activation in normal murine mammary gland epithelial cells. Tyrosine phosphorylation of p130(Cas) has been demonstrated to facilitate cell migration. We show here that tyrosine phosphorylation of paxillin alpha acts to reduce haptotactic cell migrations as well as transcellular invasive activities in several different experimental cell systems, whereas tyrosine phosphorylation of p130(Cas) exerts opposing effects to those of paxillin alpha. Each of the phosphorylation-null mutants acts as a dominant negative for each phenotype. Moreover, we found that overexpression of paxillin alpha reduced the cell saturation density of normal murine mammary gland cells, whereas overexpression of p130(Cas) increased it. These effects also seemed to depend on tyrosine phosphorylation events. Cell growth rates and morphologies at growing phases were not significantly altered, nor were cells transformed. Addition of epidermal growth factor increased saturation density of the paxillin alpha-overexpressing cells, whereas no further increment was observed in p130(Cas)-overexpressing cells. We propose that tyrosine phosphorylation of paxillin alpha and p130(Cas) exerts opposing effects on several integrin-mediated cellular events, possibly through different signaling pathways.

Indexed as

ProteinsAnimalsCell DivisionCell LineCell MovementCrk-Associated Substrate ProteinCytoskeletal ProteinsPaxillinPhosphoproteinsPhosphorylationRatsRetinoblastoma-Like Protein p130Signal TransductionTyrosineBcar1 protein, ratCrk-Associated Substrate ProteinCytoskeletal ProteinsPaxillinPhosphoproteinsProteinsPxn protein, ratRetinoblastoma-Like Protein p130Tyrosine

Identifiers

PMID10922062
PMCPMC16824
OpenAlexW2073513388

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.