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J Biol Chem, Vol. 274, Issue 9, 5782-5790, February 26, 1999

Interaction of NE-dlg/SAP102, a Neuronal and Endocrine Tissue-specific Membrane-associated Guanylate Kinase Protein, with Calmodulin and PSD-95/SAP90
A POSSIBLE REGULATORY ROLE IN MOLECULAR CLUSTERING AT SYNAPTIC SITES

Norio Masuko^§, Keishi Makino, Hiroaki Kuwahara, Kohji Fukunaga^¶, Tamotsu Sudo, Norie Araki, Hideyuki Yamamoto^¶, Yuji Yamada^§, Eishichi Miyamoto^¶, and Hideyuki Saya

From the Departments of  Tumor Genetics and Biology and ^¶ Pharmacology, Kumamoto University School of Medicine, 2-2-1, Honjo, Kumamoto 860-0811, Japan and the ^§ Cancer Research Laboratory, Hanno Research Center, Taiho Pharmaceutical Co., Ltd., 1-27, Misugidai, Hanno, Saitama 357-8527, Japan

NE-dlg/SAP102, a neuronal and endocrine tissue-specific membrane-associated guanylate kinase family protein, is known to bind to C-terminal ends of N-methyl-D-aspartate receptor 2B (NR2B) through its PDZ (PSD-95/Dlg/ZO-1) domains. NE-dlg/SAP102 and NR2B colocalize at synaptic sites in cultured rat hippocampal neurons, and their expressions increase in parallel with the onset of synaptogenesis. We have identified that NE-dlg/SAP102 interacts with calmodulin in a Ca²⁺-dependent manner. The binding site for calmodulin has been determined to lie at the putative basic -helix region located around the src homology 3 (SH3) domain of NE-dlg/SAP102. Using a surface plasmon resonance measurement system, we detected specific binding of recombinant NE-dlg/SAP102 to the immobilized calmodulin with a K_d value of 44 nM. However, the binding of Ca²⁺/calmodulin to NE-dlg/SAP102 did not modulate the interaction between PDZ domains of NE-dlg/SAP102 and the C-terminal end of rat NR2B. We have also identified that the region near the calmodulin binding site of NE-dlg/SAP102 interacts with the GUK-like domain of PSD-95/SAP90 by two-hybrid screening. Pull down assay revealed that NE-dlg/SAP102 can interact with PSD-95/SAP90 in the presence of both Ca²⁺ and calmodulin. These findings suggest that the Ca²⁺/calmodulin modulates interaction of neuronal membrane-associated guanylate kinase proteins and regulates clustering of neurotransmitter receptors at central synapses.

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