AMPA receptor trafficking and GluR1 - Response

Malinow, R., Rumpel, S., Zador, A. M., Ledoux, J. (October 2005) AMPA receptor trafficking and GluR1 - Response. Science, 310 (5746). pp. 234-235. ISSN 0036-8075

URL: https://www.ncbi.nlm.nih.gov/pubmed/16224003
DOI: 10.1126/science.310.5746.234

Abstract

In their Research Article “Postsynaptic receptor trafficking underlying a form of associative learning” (1 Apr., p. 83), S. Rumpel et al. draw the important conclusions that “encoding of memories in the lateral amygdala is mediated by AMPA receptor trafficking” and that “synaptic incorporation of AMPARs is necessary for learning.” The key experiment used to test the importance of the AMPA receptor trafficking involved the overexpression of a recombinant AMPA receptor fragment comprising 81 amino acids of the COOH-terminus of GluR1 and is referred to as the “plasticity- block” vector. This fragment is rich in protein-protein interaction sites (including PDZ, Forkhead-associated, 14-3-3 domain, and ERK and PDK docking sites) and phosphorylation sites for several kinases (PKA, PDK1, CamKII). The overexpression of this plasticity block vector will interfere with these kinases and protein interactions. Because these kinases and protein interactions are well known to regulate many synaptic (and nonsynaptic) substrates other than GluR1, it should not be assumed that only AMPA receptors are inhibited by the plasticity block vector. For example, PKA and CamKII phosphorylate multiple ion channels, enzymes, and scaffold proteins (1, 2). These experiments do not therefore prove that AMPA trafficking is either necessary or sufficient for learning. A possible conclusion would be that AMPA receptor trafficking can occur with learning, and further work is necessary before its role in learning is established.

Item Type: Paper
Uncontrolled Keywords: synaptic transmission surface expression synapses neurons actin
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > GluR1
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types
CSHL Authors:
Communities: CSHL labs > Zador lab
Depositing User: CSHL Librarian
Date: October 2005
Date Deposited: 09 Jan 2012 15:09
Last Modified: 23 Feb 2017 20:30
Related URLs:
URI: http://repository.cshl.edu/id/eprint/22643

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