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Cited by 41Neuroscience and Neuropharmacology ResearchIon channel regulation and functionProtein Kinase Regulation and GTPase Signaling

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

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Garside, M.L., Turner, P.R., Austen, B., Strehler, E.E., Beesley, P.W., Empson, R.M.·2009·Neuroscience
DOI 10.1016/j.neuroscience.2009.04.059PMC PMC2741412
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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.

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  • Ca2+ is rapidly removed from cytoplasm into extracellular space by plasma membrane calcium ATPases; ATP2B2 encodes PMCA2, whose kinetics and Ca2+ affinity make it critical to synaptic function and plasticity especially in Purkinje cell dendritic spines and parvalbumin-positive GABAergic interneurons.

    “Ca2+ is rapidly removed from the cytoplasm into the extracellular space by plasma membrane calcium ATPases (PMCAs); the ATP2B2 gene encodes for PMCA2, whose faster kinetic and broader Ca2+ affinity range makes this PMCA critical to synaptic function and plasticity especially in the dendritic spines of Purkinje cells and in parvalbumin-positive gabaergic interneurons [244–246].”

    From Consensus Paper: Pathological Role of the Cerebellum in Autism (2012) · cites this paper as [246]

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Authors
Garside, M. L., Turner, P. R., Austen, B., Strehler, E. E., Beesley, P. W., & Empson, R. M.
Affiliations
  • University of London (GB)
  • University of Otago (NZ)
  • St George's, University of London (GB)
  • Mayo Clinic (US)
Corresponding author
Empson, R.M.
ORCID
Venue
Neuroscience
Publisher
Elsevier BV
Published
2009-08
Volume
162
Issue
2
Pages
383-395
ISSN
0306-4522 (ISSN-L)
DOI
10.1016/j.neuroscience.2009.04.059
PMC
PMC2741412
OpenAlex
W2012433213
Cited by
41
References
57
Citations by year
2022: 2 · 2021: 3 · 2020: 1 · 2019: 2 · 2018: 4 · 2017: 7 · 2015: 5 · 2014: 1 · 2013: 2 · 2012: 5
FWCI
1.93
Type
journal article
Language
en
Open access
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Neuroscience (publishedVersion)
  • PubMed (publishedVersion)
  • Europe PMC (PubMed Central) (acceptedVersion)
  • PubMed Central (acceptedVersion)
  • St George's Online Research Archive (St George's University of London) (acceptedVersion)
Funders
  • Biotechnology and Biological Sciences Research Council
  • National Institute of Neurological Disorders and Stroke (NS51769, R01NS051769)
Topics
  • Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Neuroscience and Neuropharmacology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ion channel regulation and function
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
Keywords
PMCA2, cerebellum, synapses, PSD-95, NMDA receptor, NR1, NR2A, PDZ domain, syntaxin 1A, SNARE complex, calcium efflux, protein-protein interaction, granule cells
MeSH terms
Disks Large Homolog 4 Protein, Animals, Cerebellum, Immunohistochemistry, Isoenzymes, Membrane Proteins, Synapses, Synaptosomes, Blotting, Western, Receptors, N-Methyl-D-Aspartate, Rats, Wistar, Protein Structure, Tertiary, Proteomics, Immunoprecipitation, Intracellular Signaling Peptides and Proteins, Syntaxin 1, Rats, Plasma Membrane Calcium-Transporting ATPases

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