A plasma membrane Ca2+ ATPase isoform at the postsynaptic density.
Most excitatory input in the hippocampus impinges on dendritic spines. Entry of Ca(2+) 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 Ca(2+) signaling and downstream molecules. The postsynaptic density (PSD) (the most prominent subdomain within the spine) is the site of Ca(2+) entry through NMDA receptors. We here demonstrate that Ca(2+) 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 Ca(2+)-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 Ca(2+) nanodomains at subsynaptic sites. Taken together, these results suggest a novel function for PMCAs as modulators of Ca(2+) signaling at the synapse.[1]References
- A plasma membrane Ca2+ ATPase isoform at the postsynaptic density. Burette, A.C., Strehler, E.E., Weinberg, R.J. Neuroscience (2010) [Pubmed]
Annotations and hyperlinks in this abstract are from individual authors of WikiGenes or automatically generated by the WikiGenes Data Mining Engine. The abstract is from MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.About WikiGenesOpen Access LicencePrivacy PolicyTerms of Useapsburg
