Two mutations preventing PDZ-protein interactions of GluR1 have opposite effects on synaptic plasticity

Boehm, J. S., Ehrlich, I., Hsieh, H., Malinow, R. (2006) Two mutations preventing PDZ-protein interactions of GluR1 have opposite effects on synaptic plasticity. Learn Mem, 13 (5). pp. 562-5. ISSN 1072-0502 (Print)

URL: http://www.learnmem.org/cgi/content/full/13/5/562
DOI: 10.1101/lm.253506

Abstract

The regulated trafficking of GluR1 contributes significantly to synaptic plasticity, but studies addressing the function of the GluR1 C-terminal PDZ-ligand domain in this process have produced conflicting results. Here, we resolve this conflict by showing that apparently similar C-terminal mutations of the GluR1 PDZ-ligand domain result in opposite physiological phenotypes during activity- and CamKII-induced synaptic plasticity.

Item Type: Paper
Uncontrolled Keywords: Animals Ca(2+)-Calmodulin Dependent Protein Kinase metabolism Consensus Sequence genetics physiology Excitatory Postsynaptic Potentials physiology Hippocampus metabolism Ligands Mutation Neuronal Plasticity genetics physiology Protein Structure Tertiary physiology Rats Receptors AMPA genetics metabolism Synapses metabolism Synaptic Transmission genetics physiology Transfection
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > GluR1
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > mutations
organs, tissues, organelles, cell types and functions > cell types and functions > cell functions > neural plasticity
organs, tissues, organelles, cell types and functions > sub-cellular tissues: types and functions > synapse
CSHL Authors:
Depositing User: CSHL Librarian
Date Deposited: 21 Dec 2011 14:49
Last Modified: 21 Dec 2011 14:49
URI: http://repository.cshl.edu/id/eprint/22756

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