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- W2074524904 abstract "S-SCAM has a similar molecular organization to PSD-95. Both of them interact with a cell adhesion molecule, neuroligin. We previously reported that β-catenin binds S-SCAM and recruits it to synapses. We have here examined using rat primary cultured neurons whether neuroligin recruits S-SCAM to synapses or S-SCAM determines the localization of neuroligin. Overexpressed neuroligin formed larger clusters under co-expression of S-SCAM but not of PSD-95. Overexpressed neuroligin blocked synaptic accumulation of PSD-95 but not of S-SCAM. S-SCAM mutant containing the neuroligin-binding region interfered with synaptic accumulation of neuroligin and PSD-95, whereas the similar mutant of PSD-95 had no effect. Biochemical studies revealed that neuroligin forms a ternary complex with S-SCAM and PSD-95 through manifold interactions. These findings imply that S-SCAM is tethered by β-catenin to synapses and induces synaptic accumulation of neuroligin, which subsequently recruits PSD-95 to synapses." @default.
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- W2074524904 date "2004-12-01" @default.
- W2074524904 modified "2023-10-11" @default.
- W2074524904 title "Synaptic scaffolding molecule is involved in the synaptic clustering of neuroligin" @default.
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- W2074524904 doi "https://doi.org/10.1016/j.mcn.2004.08.006" @default.
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