Evidence map›Paper›PMID 24732802›Full record

ArticleMolecular and cellular biology2014

Targeted activation of conventional and novel protein kinases C through differential translocation patterns.

Xin Hui, Gregor Reither, Lars Kaestner, Peter Lipp

Open access · bronzeAbstract read
In one paragraph

Article in Molecular and cellular biology, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.

0numbers the graph read from it
0cells of the map it votes in
18citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

18 citing papers in PubMed, 30 citations in OpenAlex.

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  16. Genetically Encoded Voltage Indicators in Circulation Research.International journal of molecular sciences · 2015
    Review
  17. Article
  18. Nociceptor beta II, delta, and epsilon isoforms of PKC differentially mediate paclitaxel-induced spontaneous and evoked pain.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    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

4 authors at 1 institution in 1 country.

Xin HuiMolecular Cell Biology, Research Center for Molecular Imaging and Screening, Medical Faculty, Saarland University, Homburg/Saar, Germany.
Gregor ReitherMolecular Cell Biology, Research Center for Molecular Imaging and Screening, Medical Faculty, Saarland University, Homburg/Saar, Germany.
Lars KaestnerMolecular Cell Biology, Research Center for Molecular Imaging and Screening, Medical Faculty, Saarland University, Homburg/Saar, Germany.
Peter LippMolecular Cell Biology, Research Center for Molecular Imaging and Screening, Medical Faculty, Saarland University, Homburg/Saar, Germany peter.lipp@uks.eu.
Saarland University · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Activation of the two ubiquitous families of protein kinases, protein kinase A (PKA) and protein kinase C (PKC), is thought to be independently coupled to stimulation of Gαs and Gαq, respectively. Live-cell confocal imaging of protein kinase C fluorescent protein fusion constructs revealed that simultaneous activation of Gαs and Gαq resulted in a differential translocation of the conventional PKCα to the plasma membrane while the novel PKCδ was recruited to the membrane of the endoplasmic reticulum (ER). We demonstrate that the PKCδ translocation was driven by a novel Gαs-cyclic AMP-EPAC-RAP-PLCε pathway resulting in specific diacylglycerol production at the membrane of the ER. Membrane-specific phosphorylation sensors revealed that directed translocation resulted in phosphorylation activity confined to the target membrane. Specific stimulation of PKCδ caused phosphorylation of the inositol-1,4,5-trisphosphate receptor and dampening of global Ca(2+) signaling revealed by graded flash photolysis of caged inositol-1,4,5-trisphosphate. Our data demonstrate a novel signaling pathway enabling differential decoding of incoming stimuli into PKC isoform-specific membrane targeting, significantly enhancing the versatility of cyclic AMP signaling, thus demonstrating the possible interconnection between the PKA and PKC pathways traditionally treated independently. We thus provide novel and elementary understanding and insights into intracellular signaling events.

Indexed as

CalciumCalcium SignalingCell LineCell MembraneCyclic AMPCyclic AMP-Dependent Protein KinasesDiglyceridesEndoplasmic ReticulumEnzyme ActivationGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding Protein alpha Subunits, GsGuanine Nucleotide Exchange FactorsHEK293 CellsHumansIndolesInositol 1,4,5-Trisphosphate2-(1-(3-dimethylaminopropyl)-5-methoxyindol-3-yl)-3-(1H-indol-3-yl)maleimideCalciumCyclic AMPCyclic AMP-Dependent Protein KinasesDiglyceridesGTP-Binding Protein alpha Subunits, Gq-G11GTP-Binding Protein alpha Subunits, GsGuanine Nucleotide Exchange FactorsIndolesInositol 1,4,5-TrisphosphateInositol 1,4,5-Trisphosphate ReceptorsMaleimidesPhosphoinositide Phospholipase Cphospholipase C epsilonProtein Kinase C-alphaProtein Kinase C-deltaRAPGEF3 protein, humanRNA, Small InterferingTetradecanoylphorbol Acetate

Identifiers

PMID24732802
PMCPMC4054312
OpenAlexW2153930945

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.