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J Biol Chem, Vol. 274, Issue 17, 11889-11896, April 23, 1999

MAGUIN, a Novel Neuronal Membrane-associated Guanylate Kinase-interacting Protein

Ikuko YaoDagger , Yutaka HataDagger , Nobuyuki IdeDagger , Kazuyo HiraoDagger , Maki DeguchiDagger , Hideo NishiokaDagger , Akira Mizoguchi§, and Yoshimi TakaiDagger

From the Dagger  Takai Biotimer Project, Exploratory Research for Advanced Technology, Japan Science and Technology Corporation, c/o JCR Pharmaceuticals Co. Ltd., 2-2-10 Murotani, Nishi-ku, Kobe 651-2241, Japan, the § Department of Anatomy and Neurobiology, Graduate School, Kyoto University, Kyoto 606-8315, Japan, and the  Department of Molecular Biology and Biochemistry, Osaka University Medical School, Suita 565-0871, Japan

Postsynaptic density (PSD)-95/Synapse-associated protein (SAP) 90 and synaptic scaffolding molecule (S-SCAM) are neuronal membrane-associated guanylate kinases. Because PSD-95/SAP90 and S-SCAM function as synaptic scaffolding proteins, identification of ligands for these proteins is important to elucidate the structure of synaptic junctions. Here, we report a novel protein interacting with the PDZ domains of PSD-95/SAP90 and S-SCAM and named it MAGUIN-1 (membrane-associated guanylate kinase-interacting protein-1). MAGUIN-1 has one sterile alpha  motif, one PDZ, and one plekstrin homology domain. MAGUIN-1 is localized at the plasma membrane via the plekstrin homology domain and the C-terminal region and interacts with PSD-95/SAP90 and S-SCAM via a C-terminal PDZ domain-binding motif. MAGUIN-1 has a short isoform, MAGUIN-2, which lacks a PDZ domain-binding motif. MAGUINs are expressed in neurons and localized in the cell body and neurites and are coimmunoprecipitated with PSD-95/SAP90 and S-SCAM from rat crude synaptosome. MAGUIN-1 may play an important role with PSD-95/SAP90 and S-SCAM to assemble the components of synaptic junctions.


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

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