Boehm, J. S., Ehrlich, I., Hsieh, H., Malinow, R. (September 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)
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: | |
| Communities: | CSHL labs > Malinow lab |
| Depositing User: | CSHL Librarian |
| Date: | September 2006 |
| Date Deposited: | 21 Dec 2011 14:49 |
| Last Modified: | 12 Apr 2018 16:24 |
| Related URLs: | |
| URI: | https://repository.cshl.edu/id/eprint/22756 |
Actions (login required)
 |
Administrator's edit/view item |