Evidence map›Paper›PMID 19570980›Full record

ArticleThe Journal of biological chemistry2009

The PKARIalpha subunit of protein kinase A modulates the activation of p90RSK1 and its function.

Deepti Chaturvedi, Michael S Cohen, Jack Taunton, Tarun B Patel

Open access · hybridAbstract read
In one paragraph

Article in The Journal of biological chemistry, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
1.3field-weighted citation impact, top 18% 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

21 citing papers in PubMed, 27 citations in OpenAlex.

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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

4 authors at 2 institutions in 1 country.

Deepti ChaturvediDepartment of Pharmacology, Stritch School of Medicine, Loyola University Chicago, Maywood, Illinois 60153, USA.
Michael S Cohen
Jack Taunton
Tarun B Patel
Loyola University Chicago · USUniversity of California, San Francisco · US

Funding

Modulation of Cellular Signaling by Sprouty ProteinsR01GM073181 · NIGMS · LOYOLA UNIVERSITY CHICAGO · PI PATEL, TARUN B. · 2005 to 2008
$1.4M
Highly Selective, Irreversible Protein Kinase InhibitorsR01GM071434 · NIGMS · UNIVERSITY OF CALIFORNIA, SAN FRANCISCO · PI TAUNTON, JACK · 2005 to 2008
$1.1M
NIGMS NIH HHS GM 071434NIGMS NIH HHS GM 073181NIGMS NIH HHS R01 GM071434NIGMS NIH HHS R01 GM073181PHS HHS AHA-ID-0830411Z
6 · The paper itself

Abstract

Previously, we showed that interactions between p90(RSK1) (RSK1) and the subunits of type I protein kinase A (PKA) regulate the activity of PKA and cellular distribution of active RSK1 (Chaturvedi, D., Poppleton, H. M., Stringfield, T., Barbier, A., and Patel, T. B. (2006) Mol. Cell Biol. 26, 4586-4600). Here we examined the role of the PKARIalpha subunit of PKA in regulating RSK1 activation and cell survival. In mouse lung fibroblasts, silencing of the PKARIalpha increased the phosphorylation and activation of RSK1, but not of RSK2 and RSK3, in the absence of any stimulation. Silencing of PKARIalpha also decreased the nuclear accumulation of active RSK1 and increased its cytoplasmic content. The increased activation of RSK1 in the absence of any agonist and changes in its subcellular redistribution resulted in increased phosphorylation of its cytoplasmic substrate BAD and increased cell survival. The activity of PKA and phosphorylation of BAD (Ser-155) were also enhanced when PKARIalpha was silenced, and this, in part, contributed to increased cell survival in unstimulated cells. Furthermore, we show that RSK1, PKA subunits, D-AKAP1, and protein phosphatase 2A catalytic subunit (PP2Ac) exist in a complex, and dissociation of RSK1 from D-AKAP1 by either silencing of PKARIalpha, depletion of D-AKAP1, or by using a peptide that competes with PKARIalpha for binding to AKAPs, decreased the amount of PP2Ac in the RSK1 complex. We also demonstrate that PP2Ac is one of the phosphatases that dephosphorylates RSK, but not ERK1/2. Thus, in unstimulated cells, the increased phosphorylation and activation of RSK1 after silencing of PKARIalpha or depletion of D-AKAP1 are due to decreased association of PP2Ac in the RSK1 complex.

Indexed as

Animalsbcl-Associated Death ProteinCell LineCell SurvivalCyclic AMP-Dependent Protein Kinase RIalpha SubunitCyclic AMP-Dependent Protein KinasesEnzyme ActivationMicePhosphorylationProtein SubunitsRibosomal Protein S6 Kinases, 90-kDaBad protein, mousebcl-Associated Death ProteinCyclic AMP-Dependent Protein Kinase RIalpha SubunitCyclic AMP-Dependent Protein KinasesProtein SubunitsRibosomal Protein S6 Kinases, 90-kDaRps6ka1 protein, mouse

Identifiers

PMID19570980
PMCPMC2749142
OpenAlexW2081304464

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.