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