Evidence map›Paper›PMID 18505819›Full record

ArticleMolecular and cellular biology2008

Physiological role for phosphatidic acid in the translocation of the novel protein kinase C Apl II in Aplysia neurons.

Carole A Farah, Ikue Nagakura, Daniel Weatherill, Xiaotang Fan, Wayne S Sossin

Open access · greenAbstract read
In one paragraph

Article in Molecular and cellular biology, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.

0numbers the graph read from it
0cells of the map it votes in
13citing papers in PubMed
1.2field-weighted citation impact, top 25% 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

13 citing papers in PubMed, 23 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Bidirectional regulation of eEF2 phosphorylation controls synaptic plasticity by decoding neuronal activity patterns.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2015
    Article
  5. Article
  6. Article
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  8. Article
  9. Article
  10. PKC differentially translocates during spaced and massed training in Aplysia.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2009
    Article
  11. Article
  12. Review
  13. 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

5 authors at 2 institutions in 1 country.

Carole A FarahDepartment of Neurology and Neurosurgery, McGill University, Montreal Neurological Institute, Montreal, Quebec H3A 2B4, Canada.
Ikue Nagakura
Daniel Weatherill
Xiaotang Fan
Wayne S Sossin
McGill University · CAMontreal Neurological Institute and Hospital · CA

Funding

CIHR 12046
6 · The paper itself

Abstract

In Aplysia californica, the serotonin-mediated translocation of protein kinase C (PKC) Apl II to neuronal membranes is important for synaptic plasticity. The orthologue of PKC Apl II, PKCepsilon, has been reported to require phosphatidic acid (PA) in conjunction with diacylglycerol (DAG) for translocation. We find that PKC Apl II can be synergistically translocated to membranes by the combination of DAG and PA. We identify a mutation in the C1b domain (arginine 273 to histidine; PKC Apl II-R273H) that removes the effects of exogenous PA. In Aplysia neurons, the inhibition of endogenous PA production by 1-butanol inhibited the physiological translocation of PKC Apl II by serotonin in the cell body and at the synapse but not the translocation of PKC Apl II-R273H. The translocation of PKC Apl II-R273H in the absence of PA was explained by two additional effects of this mutation: (i) the mutation removed C2 domain-mediated inhibition, and (ii) the mutation decreased the concentration of DAG required for PKC Apl II translocation. We present a model in which, under physiological conditions, PA is important to activate the novel PKC Apl II both by synergizing with DAG and removing C2 domain-mediated inhibition.

Indexed as

Amino Acid SequenceAnimalsAplysiaCell LineDiglyceridesIsoenzymesKineticsModels, BiologicalMolecular Sequence DataMutant ProteinsNeurons, AfferentPhosphatidic AcidsPhosphoinositide Phospholipase CPhospholipase DProtein Kinase CProtein Structure, Tertiary1,2-diacylglycerol1,2-dioctanoylglycerolApl II protein kinase CDiglyceridesIsoenzymesMutant ProteinsPhosphatidic AcidsPhosphoinositide Phospholipase CPhospholipase DProtein Kinase CSerotonin

Identifiers

PMID18505819
PMCPMC2493367
OpenAlexW2142942011

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.