Evidence map›Paper›PMID 8978822›Full record

ArticleThe Journal of cell biology1996

Translocation of Src kinase to the cell periphery is mediated by the actin cytoskeleton under the control of the Rho family of small G proteins.

V J Fincham, M Unlu, V G Brunton, J D Pitts, J A Wyke, M C Frame

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1996. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 67 papers.

0numbers the graph read from it
0cells of the map it votes in
67citing papers in PubMed
3.3field-weighted citation impact, top 8% 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

67 citing papers in PubMed, 178 citations in OpenAlex.

  1. Trial
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  7. Historical retrospective of theMolecular and clinical oncology · 2020
    Review
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  9. CBFrontiers in cellular neuroscience · 2020
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  19. Engineered kinase activation reveals unique morphodynamic phenotypes and associated trafficking for Src family isoforms.Proceedings of the National Academy of Sciences of the United States of America · 2014
    Article
  20. Review

7 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 1 institution in 1 country.

V J FinchamBeatson Institute for Cancer Research, CRC Beatson Laboratories, Glasgow, Scotland.
M Unlu
V G Brunton
J D Pitts
J A Wyke
M C Frame
Cancer Research UK Scotland Institute · GB

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

We have isolated Swiss 3T3 subclones that are resistant to the mitogenic and morphological transforming effects of v-Src as a consequence of aberrant translocation of the oncoprotein under low serum conditions. In chicken embryo and NIH 3T3 fibroblasts under similar conditions, v-Src rapidly translocates from the perinuclear region to the focal adhesions upon activation of the tyrosine kinase, resulting in downstream activation of activator protein-1 and mitogen-activated protein kinase, which are required for the mitogenic and transforming activity of the oncoprotein. Since serum deprivation induces cytoskeletal disorganization in Swiss 3T3, we examined whether regulators of the cytoskeleton play a role in the translocation of v-Src, and also c-Src, in response to biological stimuli. Actin stress fibers and translocation of active v-Src to focal adhesions in quiescent Swiss 3T3 cells were restored by microinjection of activated Rho A and by serum. Double labeling with anti-Src and phalloidin demonstrated that v-Src localized along the reformed actin filaments in a pattern that would be consistent with trafficking in complexes along the stress fibers to focal adhesions. Furthermore, treatment with the actin-disrupting drug cytochalasin D, but not the microtubule-disrupting drug nocodazole, prevented v-Src translocation. In addition to v-Src, we observed that PDGF-induced, Rac-mediated membrane ruffling was accompanied by translocation of c-Src from the cytoplasm to the plasma membrane, an effect that was also blocked by cytochalasin D. Thus, we conclude that translocation of Src from its site of synthesis to its site of action at the cell membrane requires an intact cytoskeletal network and that the small G proteins of the Rho family may specify the peripheral localization in focal adhesions or along the membrane, mediated by their effects on the cytoskeleton.

Indexed as

3T3 CellsActinsAnimalsBiological TransportCalcium-Calmodulin-Dependent Protein KinasesCell DivisionCell MembraneChick EmbryoCytoskeletonGTP-Binding ProteinsMiceMicrotubulesOncogene Protein pp60(v-src)rho GTP-Binding ProteinsTranscription Factor AP-1ActinsCalcium-Calmodulin-Dependent Protein KinasesGTP-Binding ProteinsOncogene Protein pp60(v-src)rho GTP-Binding ProteinsTranscription Factor AP-1

Identifiers

PMID8978822
PMCPMC2133963
OpenAlexW2014286995

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.