Evidence map›Paper›PMID 10082579›Full record

ArticleMolecular and cellular biology1999

Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion kinase in regulation of cell motility.

S Mañes, E Mira, C Gómez-Mouton, Z J Zhao, R A Lacalle, C Martínez-A

Abstract read
In one paragraph

Article in Molecular and cellular biology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 83 papers.

0numbers the graph read from it
0cells of the map it votes in
83citing papers in PubMed
7.6field-weighted citation impact, top 2% 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

83 citing papers in PubMed, 242 citations in OpenAlex.

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  19. The Q510E mutation in Shp2 perturbs heart valve development by increasing cell migration.Journal of applied physiology (Bethesda, Md. : 1985) · 2015
    Article
  20. Review

23 more citing papers are in PubMed but not listed here.

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

6 authors at 4 institutions in 2 countries.

S MañesDepartment of Immunology and Oncology, Centro Nacional de Biotecnología, Consejo Superior de Investigaciones Científicas, Universidad Autónoma de Madrid, Campus de Cantoblanco, E-28049 Madrid, Spain. smanes@cnb.uam.es
E Mira
C Gómez-Mouton
Z J Zhao
R A Lacalle
C Martínez-A
Consejo Superior de Investigaciones Científicas · ESCentro Nacional de Biotecnología · ESUniversidad Autónoma de Madrid · ESVanderbilt University · US

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The coordinated interplay of substrate adhesion and deadhesion is necessary for cell motility. Using MCF-7 cells, we found that insulin-like growth factor I (IGF-I) induces the adhesion of MCF-7 to vitronectin and collagen in a dose- and time-dependent manner, suggesting that IGF-I triggers the activation of different integrins. On the other hand, IGF-I promotes the association of insulin receptor substrate 1 with the focal adhesion kinase (FAK), paxillin, and the tyrosine phosphatase SHP-2, resulting in FAK and paxillin dephosphorylation. Abrogation of SHP-2 catalytic activity with a dominant-negative mutant (SHP2-C>S) abolishes IGF-I-induced FAK dephosphorylation, and cells expressing SHP2-C>S show reduced IGF-I-stimulated chemotaxis compared with either mock- or SHP-2 wild-type-transfected cells. This impairment of cell migration is recovered by reintroduction of a catalytically active SHP-2. Interestingly, SHP-2-C>S cells show a larger number of focal adhesion contacts than wild-type cells, suggesting that SHP-2 activity participates in the integrin deactivation process. Although SHP-2 regulates mitogen-activated protein kinase activity, the mitogen-activated protein kinase kinase inhibitor PD-98059 has only a marginal effect on MCF-7 cell migration. The role of SHP-2 as a general regulator of cell chemotaxis induced by other chemotactic agents and integrins is discussed.

Indexed as

Cell AdhesionCell Adhesion MoleculesCell MovementChemokine CCL5Chemotactic FactorsChemotaxisCytoskeletal ProteinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesHumansInsulin-Like Growth Factor IInsulin Receptor Substrate ProteinsIntegrinsIntracellular Signaling Peptides and ProteinsModels, BiologicalNeoplasm InvasivenessCell Adhesion MoleculesChemokine CCL5Chemotactic FactorsCytoskeletal ProteinsFocal Adhesion Kinase 1Focal Adhesion Protein-Tyrosine KinasesInsulin-Like Growth Factor IInsulin Receptor Substrate ProteinsIntegrinsIntracellular Signaling Peptides and ProteinsIRS1 protein, humanPaxillinPhosphoproteinsProtein-Tyrosine KinasesProtein Tyrosine Phosphatase, Non-Receptor Type 1Protein Tyrosine Phosphatase, Non-Receptor Type 11Protein Tyrosine Phosphatase, Non-Receptor Type 6Protein Tyrosine PhosphatasesPTK2 protein, humanPTPN11 protein, humanPTPN6 protein, humanPXN protein, humanReceptor, IGF Type 1

Identifiers

PMID10082579
PMCPMC84106
OpenAlexW2122720918

What OpenQuestion holds

Texttitle and abstract
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.