Two mutations preventing PDZ-protein interactions of GluR1 have opposite effects on synaptic plasticity.
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.
Boehm
Jannic
J
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA.
Ehrlich
Ingrid
I
Hsieh
Helen
H
Malinow
Roberto
R
D000818:Animals; D017871:Calcium-Calmodulin-Dependent Protein Kinases / Q000378:metabolism; D016384:Consensus Sequence / Q000235:genetics / Q000502:physiology; D019706:Excitatory Postsynaptic Potentials / Q000502:physiology; D006624:Hippocampus / Q000378:metabolism*; D066298:In Vitro Techniques; D008024:Ligands; D009154:Mutation; D009473:Neuronal Plasticity / Q000235:genetics / Q000502:physiology*; D017434:Protein Structure, Tertiary / Q000502:physiology; D051381:Rats; D018091:Receptors, AMPA / Q000235:genetics / Q000378:metabolism*; D013569:Synapses / Q000378:metabolism*; D009435:Synaptic Transmission / Q000235:genetics / Q000502:physiology*; D014162:Transfection
D017871:Calcium-Calmodulin-Dependent Protein Kinases; D008024:Ligands; D018091:Receptors, AMPA