| Budget Amount *help |
¥12,200,000 (Direct Cost: ¥12,200,000)
Fiscal Year 2001: ¥5,400,000 (Direct Cost: ¥5,400,000)
Fiscal Year 2000: ¥6,800,000 (Direct Cost: ¥6,800,000)
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| Research Abstract |
We have investigated the molecular structures of synapses and epithelial junctions. Through this research, we have revealed the following points ;
1. Synaptic scaffolding molecule (S-SCAM) binds p-catenin. This interaction mediates the synaptic targeting of S-SCAM. We have propose the model that b-catenin is first localized at synapses by binding to cadherin, and then recruits to synapses S-SCAM, which provides scaffolds for various components.
2. Brain-enriched guanylate kinase-interacting protein (BEGAIN) is localized in the nucleus as well as at synapses. The synaptic targeting of BEGAIN is mediated by its C-terminal region, possibly by the interaction with PSD-95 and depends on NMDA receptor activity.
3. Membrane-associated guanylate kinase-interacting protein (MAGUIN) is a mammalian homolog of Drosophila Cnk, and binds to PSD-95 and S-SCAM. The synaptic targeting of MAGUIN is mediated by the pleckstrin homology domain and is independent of the interaction with PSD-95 or S-SCAM.
4. Epithelial isoform of S-SCAM named MAGI-1/BAP1 is localized on lateral membranes by its C-terminal PDZ domain.
5. A novel PDZ protein, PAPIN, binds p0071, a member of catenin family. However, the subcellular localization of PAPIN does not depend on the interaction with p0071. PAPIN is localized not only on lateral membranes but also on apical membranes. PAPIN interacts with ERBIN, which binds ErbB2 receptor, via p0071, and may be implicated in the EGF-mediated signaling pathway.
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