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rdf:type |
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lifeskim:mentions |
umls-concept:C0017262,
umls-concept:C0072899,
umls-concept:C0079883,
umls-concept:C0185117,
umls-concept:C0205148,
umls-concept:C0333117,
umls-concept:C1705241,
umls-concept:C1705242,
umls-concept:C1710082,
umls-concept:C1711351,
umls-concept:C2911684
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pubmed:issue |
6
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pubmed:dateCreated |
2001-10-19
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pubmed:abstractText |
The molecular mechanisms that control the surface expression of NMDA receptors (NMDARs) and AMPA receptors (AMPARs) are unknown. To determine the role of the intracellular C-terminal tails of glutamate receptor subunits in the synaptic targeting of AMPARs and NMDARs, we fused the tails of the AMPAR subunits, GluR1 and GluR2, and the NMDAR subunit, NR1, to the human T lymphocyte membrane protein CD8 and expressed these constructs in HEK293 cells and cultured hippocampal neurons. The GluR1 and GluR2 fusion proteins exhibited robust surface expression in the plasma membrane of neurons at synapses as did CD8 alone. In contrast, the NR1 fusion protein was retained intracellularly in both HEK293 cells and neurons because of the presence of an ER retention signal in the C1 cassette. This ER retention signal was overridden either by the addition of a PDZ domain-binding motif or by mimicking phosphorylation at a site adjacent to the retention signal. These results provide further evidence that the intracellular trafficking of AMPAR and NMDAR subunits are regulated independently at least in part because of differences in the protein-protein interactions of their intracellular C-terminal tails.
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD8,
http://linkedlifedata.com/resource/pubmed/chemical/NR1 NMDA receptor,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Sorting Signals,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, AMPA,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, N-Methyl-D-Aspartate,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Fusion Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/glutamate receptor ionotropic...,
http://linkedlifedata.com/resource/pubmed/chemical/glutamate receptor ionotropic...
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0028-3908
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
41
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
714-23
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:11640925-Animals,
pubmed-meshheading:11640925-Antigens, CD8,
pubmed-meshheading:11640925-Cell Membrane,
pubmed-meshheading:11640925-Cells, Cultured,
pubmed-meshheading:11640925-Endoplasmic Reticulum,
pubmed-meshheading:11640925-Hippocampus,
pubmed-meshheading:11640925-Humans,
pubmed-meshheading:11640925-Mutagenesis, Insertional,
pubmed-meshheading:11640925-Neurons,
pubmed-meshheading:11640925-Peptide Fragments,
pubmed-meshheading:11640925-Phosphorylation,
pubmed-meshheading:11640925-Protein Sorting Signals,
pubmed-meshheading:11640925-Protein Structure, Tertiary,
pubmed-meshheading:11640925-Rats,
pubmed-meshheading:11640925-Receptors, AMPA,
pubmed-meshheading:11640925-Receptors, N-Methyl-D-Aspartate,
pubmed-meshheading:11640925-Recombinant Fusion Proteins,
pubmed-meshheading:11640925-Synapses
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pubmed:year |
2001
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pubmed:articleTitle |
An ER retention signal explains differences in surface expression of NMDA and AMPA receptor subunits.
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pubmed:affiliation |
Nancy Pritzker Laboratory, Department of Psychiatry and Behavioral Sciences, School of Medicine, Stanford University, 1201 Welch Road, Room P105, 94304-Palo Alto, CA 5485, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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