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

Andres Barria, Dominique Muller, Victor Derkach, Leslie C. Griffith, Thomas R. Soderling

Research output: Contribution to journalArticlepeer-review

848 Scopus citations

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 α-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.

Original languageEnglish (US)
Pages (from-to)2042-2045
Number of pages4
JournalScience
Volume276
Issue number5321
DOIs
StatePublished - Jun 27 1997

ASJC Scopus subject areas

  • General

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