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  DRPEER: a motif in the extracellular vestibule conferring high Ca2+ flux rates in NMDA receptor channels.

Watanabe, J., Beck, C., Kuner, T., Premkumar, L. S., & Wollmuth, L. P. (2002). DRPEER: a motif in the extracellular vestibule conferring high Ca2+ flux rates in NMDA receptor channels. The Journal of Neuroscience: the Official Journal of the Society for Neuroscience, 22(23), 10209-10216. Retrieved from http://www.ncbi.nlm.nih.gov/pubmed/12451122.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-7D37-5 Version Permalink: http://hdl.handle.net/11858/00-001M-0000-0029-7D38-3
Genre: Journal Article
Alternative Title : DRPEER: a motif in the extracellular vestibule conferring high Ca2+ flux rates in NMDA receptor channels.

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JNeurosci_22_2002_10209.pdf (Any fulltext), 321KB
 
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 Creators:
Watanabe, Junryo, Author
Beck, Christine1, Author              
Kuner, Thomas1, 2, Author              
Premkumar, Louis S., Author
Wollmuth, Lonnie P.2, Author              
Affiliations:
1Department of Molecular Neurobiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497704              
2Department of Cell Physiology, Max Planck Institute for Medical Research, Max Planck Society, ou_1497701              

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Free keywords: glutamate receptor; fractional Ca2+ currents; Ca2+ permeability; extracellular vestibule; synaptic physiology; Ca2+ binding site
 Abstract: The high flux rate of Ca2+ through NMDA receptor (NMDAR) channels is critical for their biological function and may depend on a Ca2+ binding site in the extracellular vestibule. We screened substitutions of hydrophilic residues exposed in the vestibule and identified a cluster of charged residues and a proline, the DRPEER motif, positioned C terminal to M3, that is unique to the NR1 subunit. Charge neutralization or conversion of residues in DRPEER altered fractional Ca2+ currents in a manner consistent with its forming a binding site for Ca2+. Similarly, in a mutant channel in which all of the negative charges are neutralized (ARPAAR), the block by extracellular Ca2+ of single-channel current amplitudes is attenuated. In these same channels, the block by extracellular Mg2+is unaffected. DRPEER is located extracellularly, and its contribution to Ca2+ influx is distinct from that of the narrow constriction. We conclude that key residues in DRPEER, acting as an external binding site for Ca2+, along with a conserved asparagine in the M3 segment proper, contribute to the high fractional Ca2+ currents in these channels under physiological conditions. Therefore, these domains represent critical molecular determinants of NMDAR function in synaptic physiology.

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Language(s): eng - English
 Dates: 2002-09-242002-05-022002-09-262002-12-01
 Publication Status: Published in print
 Pages: 8
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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: 22 (23) Sequence Number: - Start / End Page: 10209 - 10216 Identifier: ISSN: 0270-6474
CoNE: https://pure.mpg.de/cone/journals/resource/954925502187_1