A plasma membrane Ca2+ ATPase isoform at the postsynaptic density

Abstract Most excitatory input in the hippocampus impinges on dendritic spines. Entry of Ca2+ into spines through NMDA receptors can trigger a sequence of biochemical reactions leading to sustained changes in synaptic efficacy. To provide specificity, dendritic spines restrict the diffusion of Ca2+...

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Bibliographic Details
Published in:Neuroscience 2010-09, Vol.169 (3), p.987-993
Main Authors: Burette, A.C, Strehler, E.E, Weinberg, R.J
Format: Article
Language:English
Subjects:
Animals
Biological and medical sciences
Ca super(2+)-transporting ATPase
Calcium - metabolism
calcium extrusion
calcium pump
dendritic spine
Dendritic Spines - enzymology
Fundamental and applied biological sciences. Psychology
Hippocampus - enzymology
Hippocampus - ultrastructure
Immunohistochemistry
Isoenzymes - metabolism
Male
Neurology
Plasma Membrane Calcium-Transporting ATPases - metabolism
postsynaptic density
Pyramidal Cells - enzymology
Pyramidal Cells - ultrastructure
Rats
Rats, Sprague-Dawley
Synapses - metabolism
Vertebrates: nervous system and sense organs
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Summary:Abstract Most excitatory input in the hippocampus impinges on dendritic spines. Entry of Ca2+ into spines through NMDA receptors can trigger a sequence of biochemical reactions leading to sustained changes in synaptic efficacy. To provide specificity, dendritic spines restrict the diffusion of Ca2+ signaling and downstream molecules. The postsynaptic density (PSD) (the most prominent subdomain within the spine) is the site of Ca2+ entry through NMDA receptors. We here demonstrate that Ca2+ can also be removed via pumps embedded in the PSD. Using light- and electron-microscopic immunohistochemistry, we find that PMCA2w, a member of the plasma membrane Ca2+ -ATPase (PMCA) family, concentrates at the PSD of most hippocampal spines. We propose that PMCA2w may be recruited into supramolecular complexes at the postsynaptic density, thus helping to regulate Ca2+ nanodomains at subsynaptic sites. Taken together, these results suggest a novel function for PMCAs as modulators of Ca2+ signaling at the synapse.
ISSN:0306-4522
1873-7544
DOI:10.1016/j.neuroscience.2010.05.062