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The Journal of Neuroscience, February 15, 1999, 19(4):1165-1178
Interactions of Calmodulin and
-Actinin with the NR1 Subunit Modulate Ca2+-Dependent Inactivation of NMDA Receptors
Johannes J. Krupp1, Bryce Vissel2, Christopher G. Thomas1, Stephen F. Heinemann2, and Gary L. Westbrook1 1 Vollum Institute, Oregon Health Sciences University, Portland, Oregon 97201, and 2 Molecular Neurobiology Laboratory, Salk Institute, La Jolla, California 92037
Glutamate receptors are associated with various regulatory and cytoskeletal proteins. However, an understanding of the functional significance of these interactions is still rudimentary. Studies in hippocampal neurons suggest that such interactions may be involved in calcium-induced reduction in the open probability of NMDA receptors (inactivation). Thus we examined the role of the intracellular domains of the NR1 subunit and two of its binding partners, calmodulin and
-actinin, on this process using NR1/NR2A heteromers expressed in human embryonic kidney (HEK) 293 cells. The presence of the first 30 residues of the intracellular C terminus of NR1 (C0 domain) was required for inactivation. Mutations in the last five residues of C0 reduced inactivation and produced parallel shifts in binding of
Key words: Ca/calmodulin;
Copyright © 1999 Society for Neuroscience 0270-6474/99/1941165-14$05.00/0
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