Evidence map›Paper›PMID 8413226›Full record

ArticleMolecular and cellular biology1993

A growth factor-induced kinase phosphorylates the serum response factor at a site that regulates its DNA-binding activity.

V M Rivera, C K Miranti, R P Misra, D D Ginty, R H Chen, J Blenis, M E Greenberg

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 1993. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 84 papers.

0numbers the graph read from it
0cells of the map it votes in
84citing papers in PubMed
8.7field-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

84 citing papers in PubMed, 252 citations in OpenAlex.

  1. Article
  2. Article
  3. Inhibition of p90 ribosomal S6 kinases disrupts melanoma cell growth and immune evasion.Journal of experimental & clinical cancer research : CR · 2023
    Article
  4. Article
  5. Article
  6. Article
  7. ERK signalling: a master regulator of cell behaviour, life and fate.Nature reviews. Molecular cell biology · 2020
    Review
  8. Article
  9. Review
  10. Emerging themes in neuronal activity-dependent gene expression.Molecular and cellular neurosciences · 2018
    Review
  11. Article
  12. Article
  13. Article
  14. The STARS signaling pathway: a key regulator of skeletal muscle function.Pflugers Archiv : European journal of physiology · 2014
    Review
  15. SRF phosphorylation by glycogen synthase kinase-3 promotes axon growth in hippocampal neurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2014
    Article
  16. The transcription factor serum response factor stimulates axon regeneration through cytoplasmic localization and cofilin interaction.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2013
    Article
  17. p90 ribosomal S6 kinase 3 contributes to cardiac insufficiency in α-tropomyosin Glu180Gly transgenic mice.American journal of physiology. Heart and circulatory physiology · 2013
    Article
  18. Article
  19. Article
  20. Article

24 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

7 authors at 1 institution in 1 country.

V M RiveraDepartment of Microbiology and Molecular Genetics, Harvard Medical School, Boston, Massachusetts 02115.
C K Miranti
R P Misra
D D Ginty
R H Chen
J Blenis
M E Greenberg
Harvard University · US

Funding

NERVE GROWTH FACTOR REGULATION OF GENE EXPRESSIONR01CA043855 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI GREENBERG, MICHAEL E · 1987 to 2001
$783k
NCI NIH HHS CA6595NCI NIH HHS R01 CA43855
6 · The paper itself

Abstract

A signaling pathway by which growth factors may induce transcription of the c-fos proto-oncogene has been characterized. Growth factor stimulation of quiescent fibroblasts activates a protein kinase cascade that leads to the rapid and transient phosphorylation of the serum response factor (SRF), a regulator of c-fos transcription. The in vivo kinetics of SRF phosphorylation and dephosphorylation parallel the activation and subsequent repression of c-fos transcription, suggesting that this phosphorylation event plays a critical role in the control of c-fos expression. The ribosomal S6 kinase pp90rsk, a growth factor-inducible kinase, phosphorylates SRF in vitro at serine 103, the site that becomes newly phosphorylated upon growth factor stimulation in vivo. Phosphorylation of serine 103 significantly enhances the affinity and rate with which SRF associates with its binding site, the serum response element, within the c-fos promoter. These results suggest a model in which the growth factor-induced phosphorylation of SRF at serine 103 contributes to the activation of c-fos transcription by facilitating the formation of an active transcription complex at the serum response element.

Indexed as

3T3 CellsAnimalsAntibodiesBase SequenceBinding SitesCell LineDNADNA-Binding ProteinsEpidermal Growth FactorHumansKineticsMiceMolecular Sequence DataNuclear ProteinsPhosphorylationPromoter Regions, GeneticAntibodiesDNADNA-Binding ProteinsEpidermal Growth FactorMAS1 protein, humanNuclear ProteinsProtein Serine-Threonine KinasesProto-Oncogene MasProto-Oncogene Proteins c-fosRibosomal ProteinsRibosomal Protein S6Ribosomal Protein S6 KinasesSerineSerum Response Factor

Identifiers

PMID8413226
PMCPMC364685
OpenAlexW1857652952

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.