Evidence map›Paper›PMID 16893971›Full record

ArticleThe Journal of cell biology2006

PKCalpha: a versatile key for decoding the cellular calcium toolkit.

Gregor Reither, Michael Schaefer, Peter Lipp

Open access · bronzeAbstract read
In one paragraph

Article in The Journal of cell biology, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 26 papers.

0numbers the graph read from it
0cells of the map it votes in
26citing papers in PubMed
3.0field-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

26 citing papers in PubMed, 64 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Striking a balance: PIPExploration of neuroprotective therapy · 2021
    Article
  5. Dietary fructose enhances angiotensin II-stimulated NaAmerican journal of physiology. Renal physiology · 2020
    Article
  6. Article
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  8. Article
  9. Article
  10. Article
  11. Article
  12. Article
  13. Article
  14. Article
  15. Review
  16. Protein kinase C: the "masters" of calcium and lipid.Cold Spring Harbor perspectives in biology · 2011
    Review
  17. Article
  18. Article
  19. Review
  20. Lipid activation of protein kinases.Journal of lipid research · 2009
    Review
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 2 institutions in 1 country.

Gregor ReitherInstitute for Molecular Cell Biology, Medical Faculty of the Saarland University, D-66421 Homburg/Saar, Germany.
Michael Schaefer
Peter Lipp
Saarland University · DECharité - Universitätsmedizin Berlin · DE

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Conventional protein kinases C (cPKCs) play an essential role in signal transduction and are believed to integrate both global Ca(2+) transients and diacylglycerol signals. We provide evidence that PKCalpha is a ubiquitous readout sensor for the cellular Ca(2+) toolkit, including highly restricted elementary Ca(2+) release. Threshold stimulations of cells with Ca(2+)-mobilizing agonists resulted in PKCalpha translocation events with limited spatial spreads (<4 microm) comprising two groups of lifetimes; brief events (400-1,500 ms) exclusively mediated by Ca(2+)-C2 domain membrane interactions and long-lasting events (>4 s) resulting from longer DAG-C1a domain-mediated membrane interactions. Although upon uncaging NP-EGTA, which is a caged Ca(2+) compound, WT-PKCalpha displayed rapid membrane translocations within <250 ms, PKCalpha constructs with C2 domains mutated in their Ca(2+)-binding region lacked any Ca(2+)-dependent translocation. Flash photolysis of diazo-2, a photosensitive caged Ca(2+) buffer, revealed a biphasic membrane dissociation (slow and fast period) of WT-PKCalpha. The slow phase was absent in cells expressing PKCalpha-constructs containing mutated C1a-domains with largely reduced DAG binding. Thus, two groups of PKCalpha membrane interactions coexist; C2- and C1a-mediated interactions with different lifetimes but rapid interconversion. We conclude that PKCalpha can readout very fast and, spatially and temporally, very complex cellular Ca(2+) signals. Therefore, cPKCs are important transducers for the ubiquitous cellular Ca(2+) signaling toolkit.

Indexed as

AnimalsBinding SitesBiosensing TechniquesCalciumCalcium SignalingCell MembraneChelating AgentsChlorocebus aethiopsCOS CellsDiglyceridesGreen Fluorescent ProteinsHumansIntracellular Calcium-Sensing ProteinsIntracellular FluidMutationProtein Kinase C-alphaCalciumChelating AgentsDiglyceridesenhanced green fluorescent proteinGreen Fluorescent ProteinsIntracellular Calcium-Sensing ProteinsProtein Kinase C-alphaRecombinant Fusion Proteins

Identifiers

PMID16893971
PMCPMC2064258
OpenAlexW2036513871

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC-SA
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.