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.

@article{Masuko1999InteractionON,
  title={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.},
  author={Norio Masuko and Keisuke Makino and Hideo Kuwahara and Kouji Fukunaga and Tatsuhiko Sudo and Nobukazu Araki and Hideki Yamamoto and Yukio Yamada and Eishichi Miyamoto and Hideyuki Saya},
  journal={The Journal of biological chemistry},
  year={1999},
  volume={274 9},
  pages={
          5782-90
        }
}
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… CONTINUE READING
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