Evidence map›Paper›PMID 7623830›Full record

ArticleMolecular and cellular biology1995

RSK3 encodes a novel pp90rsk isoform with a unique N-terminal sequence: growth factor-stimulated kinase function and nuclear translocation.

Y Zhao, C Bjørbaek, S Weremowicz, C C Morton, D E Moller

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 1995. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 52 papers.

0numbers the graph read from it
0cells of the map it votes in
52citing papers in PubMed
3.4field-weighted citation impact, top 7% 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

52 citing papers in PubMed, 139 citations in OpenAlex.

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  17. Suppression of DNA-damage checkpoint signaling by Rsk-mediated phosphorylation of Mre11.Proceedings of the National Academy of Sciences of the United States of America · 2013
    Article
  18. Review
  19. Article
  20. RSK2 Binding Models Delineate Key Features for Activity.Journal of chemical and pharmaceutical research · 2010
    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

5 authors at 2 institutions in 1 country.

Y ZhaoCharles A. Dana Research Institute, Beth Israel Hospital, Boston, Massachusetts 02215, USA.
C Bjørbaek
S Weremowicz
C C Morton
D E Moller
Harvard University · USBrigham and Women's Hospital · US

Funding

PHS HHS R01 45874-02
6 · The paper itself

Abstract

A novel pp90rsk Ser/Thr kinase (referred to as RSK3) was cloned from a human cDNA library. The RSK3 cDNA encodes a predicted 733-amino-acid protein with a unique N-terminal region containing a putative nuclear localization signal. RSK3 mRNA was widely expressed (but was predominant in lung and skeletal muscle). By using fluorescence in situ hybridization, the human RSK3 gene was localized to band q27 of chromosome 6. Hemagglutinin epitope-tagged RSK3 was expressed in transiently transfected COS cells. Growth factors, serum, and phorbol ester stimulated autophosphorylation of recombinant RSK3 and its kinase activity toward several protein substrates known to be phosphorylated by RSKs. However, the relative substrate specificity of RSK3 differed from that reported for other isoforms. RSK3 also phosphorylated potential nuclear target proteins including c-Fos and histones. Furthermore, although RSK3 was inactivated by protein phosphatase 2A in vitro, the enzyme was not activated by ERK2/mitogen-activated protein (MAP) kinase. In contrast, the kinase activity of another epitope-tagged RSK isoform (RSK-1) was significantly increased by in vitro incubation with ERK2/MAP kinase. Finally, we used affinity-purified RSK3 antibodies to demonstrate by immunofluorescence that endogenous RSK3 undergoes serum-stimulated nuclear translocation in cultured HeLa cells. These results provide evidence that RSK3 is a third distinct isoform of pp90rsk which translocates to the cell nucleus, phosphorylates potential nuclear targets, and may have a unique upstream activator. RSK3 may therefore subserve a discrete physiologic role(s) that differs from those of the other two known mammalian RSK isoforms.

Indexed as

Cell CompartmentationAmino Acid SequenceBase SequenceBiological TransportCalcium-Calmodulin-Dependent Protein KinasesCell DivisionCell NucleusChromosome MappingChromosomes, Human, Pair 6Cloning, MolecularDNA, ComplementaryGene ExpressionGrowth SubstancesHumansIn Situ Hybridization, FluorescenceIsoenzymesCalcium-Calmodulin-Dependent Protein KinasesDNA, ComplementaryGrowth SubstancesIsoenzymesMitogen-Activated Protein Kinase 1Phosphoprotein PhosphatasesProtein Phosphatase 2Protein Serine-Threonine KinasesProtein Sorting SignalsRecombinant ProteinsRibosomal Protein S6 KinasesRNA, Messenger

Identifiers

PMID7623830
PMCPMC230675
OpenAlexW2112059462

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.