WWW.JNEUROSCI.ORG
-
The Journal of Neuroscience Synaptic Systems Antibody Company
 QUICK SEARCH:   [advanced]


     
-


HOME
  |  
SEARCH  |   ARCHIVE  |   SUBSCRIBE  |   CONTACT  |   HELP

The Journal of Neuroscience, March 26, 2008, 28(13):3500-3509; doi:10.1523/JNEUROSCI.5239-07.2008

This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow Submit an eLetter
Right arrow Alert me when this article is cited
Right arrow Alert me when eLetters are posted
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Google Scholar
Right arrow Articles by Horak, M.
Right arrow Articles by Wenthold, R. J.
PubMed
Right arrow PubMed Citation
Right arrow Articles by Horak, M.
Right arrow Articles by Wenthold, R. J.

 Previous Article  |  Next Article 

Cellular/Molecular
Masking of the Endoplasmic Reticulum Retention Signals during Assembly of the NMDA Receptor

Martin Horak, Kai Chang, and Robert J. Wenthold

Laboratory of Neurochemistry, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, Bethesda, Maryland 20892

Correspondence should be addressed to Martin Horak, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, 50 South Drive, Room 4146, Bethesda, Maryland 20892. Email: horakm{at}nidcd.nih.gov

NMDA receptors are glutamate-gated ion channels that play important roles in synaptic transmission and excitotoxicity. The functional NMDA receptor is thought to be a heterotetramer composed mainly of two NR1 and two NR2 subunits. Although it is generally accepted that only correctly assembled NMDA receptors can pass the ER quality control, the mechanism underlying this process is not well understood. Using truncated and chimeric NMDA receptor subunits expressed in heterologous cells and cortical neurons, we found that the third membrane domains (M3) of both NR1 and NR2B contain signals that cause the unassembled subunits to be retained in the ER. M3 of both NR1 and NR2B and, M4 of NR1, are necessary for masking ER retention signals found in M3. Thus, our data reveal a critical role of the membrane domains in the assembly of functional NMDA receptors.

Key words: glutamate receptors; ion channel assembly; subunit interaction; ER retention; masking; intracellular trafficking


Received Nov. 26, 2007; revised Feb. 19, 2008; accepted Feb. 21, 2008.

Correspondence should be addressed to Martin Horak, National Institute on Deafness and Other Communication Disorders, National Institutes of Health, 50 South Drive, Room 4146, Bethesda, Maryland 20892. Email: horakm{at}nidcd.nih.gov






-

Home  |   Search  |   Archive  |   Subscribe  |   Contact  |   Help

-
Copyright 2008 by Society for Neuroscience ONLINE ISSN: 1529-2401
-