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Volume 272, Number 52, Issue of December 26, 1997
pp. 32727-32730
(Received for publication, September 11, 1997, and in revised form, October 25, 1997)
From the Vollum Institute, Oregon Health Sciences University,
Portland, Oregon 97201
Ca2+/CaM-dependent
protein kinase II (CaM-KII) can phosphorylate and potentiate responses
of
COMMUNICATION:
Identification of the
Ca2+/Calmodulin-dependent Protein Kinase II
Regulatory Phosphorylation Site in the
-Amino-3-hydroxyl-5-methyl4-isoxazole-propionate-type Glutamate
Receptor
-amino3-hydroxyl-5-methyl-4-isoxazole-propionate-type glutamate receptors in a number of systems, and recent studies implicate this mechanism in long term potentiation, a cellular model of
learning and memory. In this study we have identified this CaM-KII
regulatory site using deletion and site-specific mutants of glutamate
receptor 1 (GluR1). Only mutations affecting Ser831 altered
the 32P peptide maps of GluR1 from HEK-293 cells
co-expressing an activated CaM-KII. Likewise, when CaM-KII was infused
into cells expressing GluR1, the Ser831 to Ala mutant
failed to show potentiation of the GluR1 current. The
Ser831 site is specific to GluR1, and CaM-KII did not
phosphorylate or potentiate current in cells expressing GluR2,
emphasizing the importance of the GluR1 subunit in this regulatory
mechanism. Because Ser831 has previously been identified as
a protein kinase C phosphorylation site (Roche, K. W., O'Brien,
R. J., Mammen, A. L., Bernhardt, J., and Huganir, R. L. (1996) Neuron 16, 1179-1188), this raises the possibility
of synergistic interactions between CaM-KII and protein kinase C in
regulating synaptic plasticity.
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