Evidence map›Paper›PMID 1328860›Full record

ArticleMolecular and cellular biology1992

Jun is phosphorylated by several protein kinases at the same sites that are modified in serum-stimulated fibroblasts.

S J Baker, T K Kerppola, D Luk, M T Vandenberg, D R Marshak, T Curran, C Abate

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In one paragraph

Article in Molecular and cellular biology, 1992. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.

0numbers the graph read from it
0cells of the map it votes in
46citing papers in PubMed
9.0field-weighted citation impact, top 1% 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

46 citing papers in PubMed, 123 citations in OpenAlex.

  1. Review
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  9. ERK-associated changes of AP-1 proteins during fear extinction.Molecular and cellular neurosciences · 2011
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  11. Review
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  13. Article
  14. The functional contrariety of JNK.Molecular carcinogenesis · 2007
    Review
  15. Article
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  17. Article
  18. Article
  19. 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

7 authors at 3 institutions in 1 country.

S J BakerDepartment of Molecular Oncology and Virology, Roche Institute of Molecular Biology, Nutley, New Jersey 07110.
T K Kerppola
D Luk
M T Vandenberg
D R Marshak
T Curran
C Abate
Cold Spring Harbor Laboratory · USLa Roche College · USMolecular Oncology (United States) · US

Funding

VIRAL TRANSACTIVATIONP01CA013106 · NCI · COLD SPRING HARBOR LABORATORY · PI William Richard McCombie · 1985 to 2026
$116.8M
NCI NIH HHS CA 13106
6 · The paper itself

Abstract

c-jun is a member of the family of immediate-early genes whose expression is induced by factors such as serum stimulation, phorbol ester, and differentiation signals. Here we show that increased Jun synthesis after serum stimulation is accompanied by a concomitant increase in phosphorylation. Several serine-threonine kinases were evaluated for their ability to phosphorylate Jun in vitro. p34cdc2, protein kinase C, casein kinase II, and pp44mapk phosphorylated Jun efficiently, whereas cyclic AMP-dependent protein kinase and glycogen synthase kinase III did not. The sites phosphorylated by p34cdc2 were similar to those phosphorylated in vivo after serum induction. The major sites of phosphorylation were mapped to serines 63, 73, and 246. Phosphorylation of full-length Jun with several kinases did not affect the DNA-binding activity of Jun homodimers or Fos-Jun heterodimers. Comparison of the DNA binding and in vitro transcription properties of wild-type and mutated proteins containing either alanine or aspartic acid residues in place of Ser-63, -73, and -246 revealed only minor differences among homodimeric complexes and no differences among Fos-Jun heterodimers. Thus, phosphorylation of Jun did not produce a significant change in dimerization, DNA-binding, or in vitro transcription activity. The regulatory role of phosphorylation in the modulation of Jun function is likely to be considerably more complex than previously suggested.

Indexed as

BloodCalcium-Calmodulin-Dependent Protein KinasesCasein KinasesCDC2 Protein KinaseDNADNA Mutational AnalysisFibroblastsGlycogen Synthase KinasesHeLa CellsHumansPhosphorylationProtein BindingProtein Kinase CProtein KinasesProto-Oncogene Proteins c-junSerineCalcium-Calmodulin-Dependent Protein KinasesCasein KinasesCDC2 Protein KinaseDNAGlycogen Synthase KinasesProtein Kinase CProtein KinasesProto-Oncogene Proteins c-junSerine

Identifiers

PMID1328860
PMCPMC360396
OpenAlexW2209468787

What OpenQuestion holds

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Read underepoch 390

Registered trials

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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.