Evidence map›Paper›PMID 8063859›Full record

ArticleThe Journal of cell biology1994

Serum-induced signal transduction determines the peripheral location of beta-actin mRNA within the cell.

M A Hill, L Schedlich, P Gunning

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 1994. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.1field-weighted citation impact, top 5% 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

27 citing papers in PubMed, 91 citations in OpenAlex.

  1. Microtubules in cell migration.Essays in biochemistry · 2019
    Review
  2. Posttranscriptional and Posttranslational Regulation of Actin.Anatomical record (Hoboken, N.J. : 2007) · 2018
    Review
  3. Article
  4. Article
  5. Article
  6. Control of cytoplasmic mRNA localization.Cellular and molecular life sciences : CMLS · 2012
    Review
  7. Article
  8. Actin cytoskeleton in myofibroblast differentiation: ultrastructure defining form and driving function.Translational research : the journal of laboratory and clinical medicine · 2011
    Review
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
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  17. Article
  18. The physiological significance of beta -actin mRNA localization in determining cell polarity and directional motility.Proceedings of the National Academy of Sciences of the United States of America · 2001
    Article
  19. Small, efficient hammerhead ribozymes.Molecular biotechnology · 2000
    Article
  20. Article
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

3 authors at 1 institution in 1 country.

M A HillCell Biology Unit, Children's Medical Research Institute, New South Wales, Australia.
L Schedlich
P Gunning
Children's Medical Research Institute · AU

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Cell motility is dependent upon the reorganization of the cellular cytoskeleton. Actin filaments form the major component of the cytoskeleton and respond rapidly to serum growth factors. We have previously shown that myoblasts sort the two cytoskeletal beta- and gamma-actin isoform mRNAs to different intracellular regions and that only beta-actin mRNA was associated with peripheral regions of cell motility (Hill, M.A. and P. Gunning. 1993. J. Cell Biol. 122: 825-832). We now show by in situ hybridization that 3T3 fibroblasts similarly sort actin isoform mRNAs and that peripheral beta-actin mRNA is regulated by serum. In the absence of serum, we could not detect beta-actin mRNA at the periphery. Addition of serum rapidly redistributed beta-actin mRNA to the periphery. gamma-actin mRNA distribution was not altered by serum addition at any time. Both proteins, as identified by immunochemistry with isoform-specific antibodies, were found in similar cellular structures. Serum-stimulated cell motility is mediated through the GTPase signal transduction pathway. We find that an RNA-binding protein, p62, that is part of this pathway, displays a localization pattern similar to beta-actin mRNA. Our results suggest a new biological mechanism which integrates signal transduction with the supply of an architectural component required for membrane remodeling. We propose that active transport of beta-actin mRNA to regions of cell motility is one possible objective of these signal transduction pathways.

Indexed as

3T3 CellsActinsAnimalsCell CompartmentationDNA-Binding ProteinsGene ExpressionGrowth SubstancesIn Situ HybridizationLysophospholipidsMicePhosphoproteinsPlatelet-Derived Growth FactorRNA-Binding ProteinsRNA, MessengerSignal TransductionActinsDNA-Binding ProteinsDok1 protein, mouseGAP-associated protein p62Growth SubstancesLysophospholipidsPhosphoproteinsPlatelet-Derived Growth FactorRNA-Binding ProteinsRNA, Messenger

Identifiers

PMID8063859
PMCPMC2120154
OpenAlexW2044028282

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.