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J Biol Chem, Vol. 274, Issue 39, 27573-27577, September 24, 1999

A Relationship between Protein Kinase C Phosphorylation and Calmodulin Binding to the Metabotropic Glutamate Receptor Subtype 7

Yoshiaki NakajimaDagger , Tomomi YamamotoDagger , Tatsuo Nakayama§, and Shigetada NakanishiDagger

From the Dagger  Department of Cell Physiology, National Institute for Physiological Sciences, Okazaki 444-8585, the § Department of Biochemistry, Miyazaki Medical College, Kiyotake, Miyazaki 889-1692, and the  Department of Biological Sciences, Kyoto University Faculty of Medicine, Kyoto 606-8501, Japan

Metabotropic glutamate receptor subtype 7 (mGluR7) is coupled to the inhibitory cyclic AMP cascade and is selectively activated by a glutamate analogue, L-2-amino-4-phosphonobutyrate. Among L-2-amino-4-phosphonobutyrate-sensitive mGluR subtypes, mGluR7 is highly concentrated at the presynaptic terminals and is thought to play an important role in modulation of glutamatergic synaptic transmission by presynaptic inhibition of glutamate release. To gain further insight into the intracellular signaling mechanisms of mGluR7, with the aid of glutathione S-transferase fusion affinity chromatography, we attempted to identify proteins that interact with the intracellular carboxyl terminus of mGluR7. Here, we report that calmodulin (CaM) directly binds to the carboxyl terminus of mGluR7 in a Ca2+-dependent manner. The CaM-binding domain is located immediately following the 7th transmembrane segment. We also show that the CaM-binding domain of mGluR7 is phosphorylated by protein kinase C (PKC). This phosphorylation is inhibited by the binding of Ca2+/CaM to the receptor. Conversely, the Ca2+/CaM binding is prevented by PKC phosphorylation. Collectively, these results suggest that mGluR7 serves to cross-link the cyclic AMP, Ca2+, and PKC phosphorylation signal transduction cascades.

Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.


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