Evidence map›Paper›PMID 1545823›Full record

ArticleMolecular and cellular biology1992

Nuclear localization and regulation of erk- and rsk-encoded protein kinases.

R H Chen, C Sarnecki, J Blenis

Open access · greenAbstract read
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 374 papers.

0numbers the graph read from it
0cells of the map it votes in
374citing papers in PubMed
27.0field-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

374 citing papers in PubMed, 1,096 citations in OpenAlex.

  1. Article
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  5. Review
  6. Protein Kinases in Obesity, and the Kinase-Targeted Therapy.Advances in experimental medicine and biology · 2024
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  8. Review
  9. The Pathogenesis of Diabetes.International journal of molecular sciences · 2023
    Review
  10. Article
  11. [Apolipoprotein E enhances migration of endometrial cancer cells byactivating the ERK/MMP9 signaling pathway].Nan fang yi ke da xue xue bao = Journal of Southern Medical University · 2023
    Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Article
  17. Review
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  20. Article

314 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

3 authors at 1 institution in 1 country.

R H ChenDepartment of Cellular and Molecular Physiology, Harvard Medical School, Boston, Massachusetts 02115.
C Sarnecki
J Blenis
Harvard University · US

Funding

ONCOGENIC REGULATION OF S6 PROTEIN KINASE &CELL GROWTHR01CA046595 · NCI · WEILL MEDICAL COLL OF CORNELL UNIV · PI JOHN BLENIS · 1988 to 2026
$10.6M
Mitogenic and Oncogenic Regulation of ERK/RSK SignalingR37CA046595 · NCI · HARVARD UNIVERSITY (MEDICAL SCHOOL) · PI BLENIS, JOHN · 2003 to 2012
$6.4M
NCI NIH HHS CA-46595
6 · The paper itself

Abstract

We demonstrate that members of the erk-encoded family of mitogen-activated protein (MAP) kinases (pp44/42mapk/erk) and members of the rsk-encoded protein kinases (RSKs or pp90rsk) are present in the cytoplasm and nucleus of HeLa cells. Addition of growth factors to serum-deprived cells results in increased tyrosine and threonine phosphorylation and in the activation of cytosolic and nuclear MAP kinases. Activated MAP kinases then phosphorylate (serine/threonine) and activate RSKs. Concurrently, a fraction of the activated MAP kinases and RSKs enter the nucleus. In addition, a distinct growth-regulated RSK-kinase activity (an enzyme[s] that phosphorylates recombinant RSK in vitro and that may be another member of the erk-encoded family of MAP kinases) was found associated with a postnuclear membrane fraction. Regulation of nuclear MAP kinase and RSK activities by growth factors and phorbol ester is coordinate with immediate-early gene expression. Indeed, in vitro, MAP kinase and/or RSK phosphorylates histone H3 and the recombinant c-Fos and c-Jun polypeptides, transcription factors phosphorylated in a variety of cells in response to growth stimuli. These in vitro studies raise the possibility that the MAP kinase/RSK signal transduction pathway represents a protein-Tyr/Ser/Thr phosphorylation cascade with the spatial distribution and temporal regulation that can account for the rapid transmission of growth-regulating information from the membrane, through the cytoplasm, and to the nucleus.

Indexed as

Gene Expression Regulation, EnzymologicRibosomal Protein S6 Kinases, 90-kDaAmino Acid SequenceCalcium-Calmodulin-Dependent Protein KinasesCell DivisionCell FractionationCell NucleusCytosolFluorescent Antibody TechniqueHeLa CellsHumansImmunoblottingMolecular Sequence DataProtein KinasesProteinsProtein-Tyrosine KinasesCalcium-Calmodulin-Dependent Protein KinasesProtein KinasesProteinsProtein-Tyrosine Kinasesribosomal protein S6 kinase, 90kDa, polypeptide 3Ribosomal Protein S6 Kinases, 90-kDaRPS6KA1 protein, human

Identifiers

PMID1545823
PMCPMC369523
OpenAlexW1821277660

What OpenQuestion holds

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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.