Evidence map›Paper›PMID 19861495›Full record

ArticleJournal of cell science2009

Distinct roles for Crk adaptor isoforms in actin reorganization induced by extracellular signals.

Susumu Antoku, Bruce J Mayer

Open access · greenAbstract read
In one paragraph

Article in Journal of cell science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
1.8field-weighted citation impact, top 16% 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

35 citing papers in PubMed, 57 citations in OpenAlex.

  1. Article
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  6. Review
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  12. The Crk adapter protein is essential forMolecular biology of the cell · 2019
    Article
  13. PEAK3/C19orf35 pseudokinase, a new NFK3 kinase family member, inhibits CrkII through dimerization.Proceedings of the National Academy of Sciences of the United States of America · 2019
    Article
  14. Article
  15. Article
  16. Article
  17. Src homology 2 domains enhance tyrosine phosphorylationThe Journal of biological chemistry · 2018
    Article
  18. Article
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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

2 authors at 1 institution in 1 country.

Susumu AntokuDepartment of Genetics and Developmental Biology, University of Connecticut Health Center, Farmington, CT 06030-3301, USA.
Bruce J Mayer
UConn Health · US

Funding

Functional Role of NCK and CRK Binding InteractionsR01CA082258 · NCI · UNIVERSITY OF CONNECTICUT SCH OF MED/DNT · PI MAYER, BRUCE J. · 1999 to 2012
$4.2M
NCI NIH HHS CA82258NCI NIH HHS R01 CA082258
6 · The paper itself

Abstract

Crk family adaptors, consisting of Src homology 2 (SH2) and SH3 protein-binding domains, mediate assembly of protein complexes in signaling. CrkI, an alternately spliced form of Crk, lacks the regulatory phosphorylation site and C-terminal SH3 domain present in CrkII and CrkL. We used gene silencing combined with mutational analysis to probe the role of Crk adaptors in platelet-derived growth-factor receptor beta (PDGFbetaR) signaling. We demonstrate that Crk adaptors are required for formation of focal adhesions, and for PDGF-stimulated remodeling of the actin cytoskeleton and cell migration. Crk-dependent signaling is crucial during the early stages of PDGFbetaR activation, whereas its termination by Abl family tyrosine kinases is important for turnover of focal adhesions and progression of dorsal-membrane ruffles. CrkII and CrkL preferentially activate the small GTPase Rac1, whereas variants lacking a functional C-terminal SH3 domain, including CrkI, preferentially activate Rap1. Thus, differences in the activity of Crk isoforms, including their effectors and their ability to be downregulated by phosphorylation, are important for coordinating dynamic changes in the actin cytoskeleton in response to extracellular signals.

Indexed as

Actin CytoskeletonActinsAdaptor Proteins, Signal TransducingAnimalsCell LineCell MembraneCell MovementFocal AdhesionsGene SilencingHumansMiceNuclear ProteinsPhosphorylationProtein IsoformsProto-Oncogene Proteins c-ablProto-Oncogene Proteins c-crkActinsAdaptor Proteins, Signal TransducingCRKL proteinCRK protein, humanNuclear ProteinsProtein IsoformsProto-Oncogene Proteins c-ablProto-Oncogene Proteins c-crkrac1 GTP-Binding Proteinrap1 GTP-Binding ProteinsReceptor, Platelet-Derived Growth Factor beta

Identifiers

PMID19861495
PMCPMC2776506
OpenAlexW2161376583

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.