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Synaptic scaffolding molecule (S‐SCAM) membrane‐associated guanylate kinase with inverted organization (MAGI)‐2 is associated with cell adhesion molecules at inhibitory synapses in rat hippocampal neurons
Author(s) -
Sumita Kazutaka,
Sato Yuji,
Iida Junko,
Kawata Akira,
Hamano Mamiko,
Hirabayashi Susumu,
Ohno Kikuo,
Peles Elior,
Hata Yutaka
Publication year - 2007
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.2006.04170.x
Subject(s) - neuroligin , guanylate kinase , neurexin , pdz domain , gephyrin , inhibitory postsynaptic potential , microbiology and biotechnology , biology , hippocampal formation , synaptogenesis , excitatory postsynaptic potential , chemistry , neuroscience , biochemistry , receptor , postsynaptic potential , membrane protein , glycine receptor , amino acid , membrane , glycine
Synaptic scaffolding molecule (S‐SCAM) is a synaptic protein, which harbors five or six PSD‐95/Discs large/ZO‐1 (PDZ), a guanylate kinase and two WW domains. It interacts with NMDA receptor subunits, neuroligin and β‐catenin, and is involved in the accumulation of neuroligin at excitatory synapses. In this study, we have demonstrated S‐SCAM is localized at inhibitory synapses in rat primary cultured hippocampal neurons. We have identified β‐dystroglycan (β‐DG) as a binding partner for S‐SCAM at inhibitory synapses. WW domains of S‐SCAM bind to three sequences of β‐DG. We have also revealed that S‐SCAM can interact with neuroligin 2, which is known to be exclusively localized at inhibitory synapses. The WW domains and the second PDZ domain of S‐SCAM are involved in the interaction with neuroligin 2. β‐DG, neuroligin 2 and S‐SCAM form a tripartite complex in vitro . Neuroligin 2 is detected in the immunoprecipitates by anti‐β‐DG antibody from rat brain. S‐SCAM, β‐DG and neuroligin 2 are partially co‐localized in rat hippocampal neurons. These data suggest that S‐SCAM is associated with β‐DG and neuroligin 2 at inhibitory synapses, and functions as a linker between the dystrophin glycoprotein complex and the neurexin–neuroligin complex.