Evidence map›Paper›PMID 19406213›Full record

ArticleNeuroscience2009

Molecular interactions of the plasma membrane calcium ATPase 2 at pre- and post-synaptic sites in rat cerebellum.

M L Garside, P R Turner, B Austen, E E Strehler, P W Beesley, R M Empson

Abstract read
In one paragraph

Article in Neuroscience, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.

0numbers the graph read from it
0cells of the map it votes in
23citing papers in PubMed
1.6field-weighted citation impact, top 20% 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

23 citing papers in PubMed, 39 citations in OpenAlex.

  1. Article
  2. Crosstalk among Calcium ATPases: PMCA, SERCA and SPCA in Mental Diseases.International journal of molecular sciences · 2021
    Review
  3. Article
  4. The Puzzling Role of Neuron-Specific PMCA Isoforms in the Aging Process.International journal of molecular sciences · 2019
    Review
  5. Article
  6. Review
  7. Hydrodynamics govern the pre-fusion docking time of synaptic vesicles.Journal of the Royal Society, Interface · 2018
    Article
  8. Review
  9. Article
  10. The neuronal porosome complex in health and disease.Experimental biology and medicine (Maywood, N.J.) · 2016
    Review
  11. Article
  12. Article
  13. Plasma membrane calcium ATPases as novel candidates for therapeutic agent development.Journal of pharmacy & pharmaceutical sciences : a publication of the Canadian Society for Pharmaceutical Sciences, Societe canadienne des sciences pharmaceutiques · 2013
    Review
  14. Review
  15. Article
  16. PMCA2 via PSD-95 controls calcium signaling by α7-containing nicotinic acetylcholine receptors on aspiny interneurons.The Journal of neuroscience : the official journal of the Society for Neuroscience · 2012
    Article
  17. Calcium signaling in dendritic spines.Cold Spring Harbor perspectives in biology · 2012
    Article
  18. Plasma membrane calcium pumps and their emerging roles in cancer.World journal of biological chemistry · 2010
    Article
  19. Article
  20. 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

6 authors at 4 institutions in 3 countries.

M L GarsideSchool of Biological Sciences, Royal Holloway College, University of London, Egham TW20 0EX, UK.
P R Turner
B Austen
E E Strehler
P W Beesley
R M Empson
Royal Holloway University of London · GBMayo Clinic · USSt George's, University of London · GBUniversity of Otago · NZ

Funding

Membrane Targeting of Calcium-Pumping ATPaseR01NS051769 · NINDS · MAYO CLINIC ROCHESTER · PI STREHLER, EMANUEL ERNST · 2007 to 2010
$1.4M
Biotechnology and Biological Sciences Research CouncilNINDS NIH HHS NS51769NINDS NIH HHS R01 NS051769
6 · The paper itself

Abstract

The plasma membrane calcium extrusion mechanism, PMCA (plasma membrane calcium ATPase) isoform 2 is richly expressed in the brain and particularly the cerebellum. Whilst PMCA2 is known to interact with a variety of proteins to participate in important signalling events [Strehler EE, Filoteo AG, Penniston JT, Caride AJ (2007) Plasma-membrane Ca(2+) pumps: structural diversity as the basis for functional versatility. Biochem Soc Trans 35 (Pt 5):919-922], its molecular interactions in brain synapse tissue are not well understood. An initial proteomics screen and a biochemical fractionation approach identified PMCA2 and potential partners at both pre- and post-synaptic sites in synapse-enriched brain tissue from rat. Reciprocal immunoprecipitation and GST pull-down approaches confirmed that PMCA2 interacts with the post-synaptic proteins PSD95 and the NMDA glutamate receptor subunits NR1 and NR2a, via its C-terminal PDZ (PSD95/Dlg/ZO-1) binding domain. Since PSD95 is a well-known partner for the NMDA receptor this raises the exciting possibility that all three interactions occur within the same post-synaptic signalling complex. At the pre-synapse, where PMCA2 was present in the pre-synapse web, reciprocal immunoprecipitation and GST pull-down approaches identified the pre-synaptic membrane protein syntaxin-1A, a member of the SNARE complex, as a potential partner for PMCA2. Both PSD95-PMCA2 and syntaxin-1A-PMCA2 interactions were also detected in the molecular and granule cell layers of rat cerebellar sagittal slices by immunohistochemistry. These specific molecular interactions at cerebellar synapses may allow PMCA2 to closely control local calcium dynamics as part of pre- and post-synaptic signalling complexes.

Indexed as

AnimalsBlotting, WesternCerebellumDisks Large Homolog 4 ProteinImmunohistochemistryImmunoprecipitationIntracellular Signaling Peptides and ProteinsIsoenzymesMembrane ProteinsPlasma Membrane Calcium-Transporting ATPasesProtein Structure, TertiaryProteomicsRatsRats, WistarReceptors, N-Methyl-D-AspartateSynapsesDisks Large Homolog 4 ProteinDlg4 protein, ratIntracellular Signaling Peptides and ProteinsIsoenzymesMembrane ProteinsNR1 NMDA receptorNR2A NMDA receptorPlasma Membrane Calcium-Transporting ATPasesReceptors, N-Methyl-D-AspartateStx1a protein, ratSyntaxin 1

Identifiers

PMID19406213
PMCPMC2741412
OpenAlexW2012433213

What OpenQuestion holds

Textmetadata
LicenceTDM
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.