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Title

Regulatory phosphorylation of AMPA-type glutamate receptors by CaM-KII during long-term potentiation

Authors
Barria, A.
Derkach, V.
Griffith, L. C.
Soderling, T. R.
Published in Science. 1997, vol. 276, no. 5321, p. 2042-2045
Abstract Long-term potentiation (LTP), a cellular model of learning and memory, requires calcium-dependent protein kinases. Induction of LTP increased the phosphorus-32 labeling of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA)-type glutamate receptors (AMPA-Rs), which mediate rapid excitatory synaptic transmission. This AMPA-R phosphorylation appeared to be catalyzed by Ca2+- and calmodulin-dependent protein kinase II (CaM-KII): (i) it correlated with the activation and autophosphorylation of CaM-KII, (ii) it was blocked by the CaM-KII inhibitor KN-62, and (iii) its phosphorus-32 peptide map was the same as that of GluR1 coexpressed with activated CaM-KII in HEK-293 cells. This covalent modulation of AMPA-Rs in LTP provides a postsynaptic molecular mechanism for synaptic plasticity.
Keywords AnimalsCalcium/metabolismCalcium-Calmodulin-Dependent Protein Kinase Type 2Calcium-Calmodulin-Dependent Protein Kinases/antagonists & inhibitors/ metabolismCell LineEnzyme Inhibitors/pharmacologyExcitatory Amino Acid Antagonists/pharmacologyHippocampus/ metabolismHumansLong-Term Potentiation/drug effectsMalePeptide MappingPhosphorylationRatsRats, Sprague-DawleyReceptors, AMPA/ metabolismSynaptic Transmission/drug effects
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Other version: http://www.sciencemag.org/cgi/reprint/276/5321/2042.pdf
Identifiers
PMID: 9197267
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