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  C-terminal truncation of NR2A subunits impairs synaptic but not extrasynaptic localization of NMDA receptors

Steigerwald, F., Schulz, T. W., Schenker, L. T., Kennedy, M. B., Seeburg, P. H., & Köhr, G. (2000). C-terminal truncation of NR2A subunits impairs synaptic but not extrasynaptic localization of NMDA receptors. The Journal of Neuroscience: the Official Journal of the Society for Neuroscience, 20(12), 4573-4581. Retrieved from http://www.jneurosci.org/cgi/content/abstract/20/12/4573?maxtoshow%3D%26HITS%3D10%26hits%3D10%26RESULTFORMAT%3D%26searchid%3D1028657727087_4562%26stored_search%3D%26FIRSTINDEX%3D0%26volume%3D20%26firstpage%3D4573%26journalcode%3Djneuro.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-2EDE-C Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0028-2EDF-A
Genre: Journal Article
Alternative Title : C-terminal truncation of NR2A subunits impairs synaptic but not extrasynaptic localization of NMDA receptors

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JNeurosci_20_2000_4573.pdf (Any fulltext), 428KB
 
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Steigerwald, Frank1, Author              
Schulz, Torsten Wilhelm1, Author              
Schenker, Leslie T., Author
Kennedy, Mary B., Author
Seeburg, Peter H.1, Author              
Köhr, Georg1, Author              
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              

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Free keywords: immunocytochemistry; Western blotting; patch clamp; hippocampal culture and slice; mice expressing C-terminally truncated NR2A subunits; nucleated patches; evoked EPSCs; miniature currents; NR2B−specific antagonists (CP−101,606)
 Abstract: NMDA receptors interact via the extended intracellular C-terminal domain of the NR2 subunits with constituents of the postsynaptic density for purposes of retention, clustering, and functional regulation at central excitatory synapses. To examine the role of the C-terminal domain of NR2A in the synaptic localization and function of NR2A-containing NMDA receptors in hippocampal Schaffer collateral–CA1 pyramidal cell synapses, we analyzed mice which express NR2A only in its C-terminally truncated form. In CA1 cell somata, the levels, activation, and deactivation kinetics of extrasynaptic NMDA receptor channels were comparable in wild-type and mutant NR2AΔ C/ Δ Cmice. At CA1 cell synapses, however, the truncated receptors were less concentrated than their full-length counterparts, as indicated by immunodetection in cultured neurons, synaptosomes, and postsynaptic densities. In the mutant, the NMDA component of evoked EPSCs was reduced in a developmentally progressing manner and was even more reduced in miniature EPSCs (mEPSCs) elicited by spontaneous glutamate release. Moreover, pharmacologically isolated NMDA currents evoked by synaptic stimulation had longer latencies and displayed slower rise and decay times, even in the presence of an NR2B-specific antagonist. These data strongly suggest that the C-terminal domain of NR2A subunits is important for the precise synaptic arrangement of NMDA receptors.

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Language(s): eng - English
 Dates: 2000-03-312000-01-272000-04-072000-06-15
 Publication Status: Published in print
 Pages: 9
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 Table of Contents: -
 Rev. Type: Peer
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Title: The Journal of Neuroscience : the Official Journal of the Society for Neuroscience
  Other : J. Neurosci.
Source Genre: Journal
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Publ. Info: Baltimore, MD : The Society
Pages: - Volume / Issue: 20 (12) Sequence Number: - Start / End Page: 4573 - 4581 Identifier: ISSN: 0270-6474
CoNE: https://pure.mpg.de/cone/journals/resource/954925502187_1