| Research Abstract |
The synaptic protein PSD95/SAP90 interacts with ion channels such as the N-methyl-D-aspartate-receptor (NMDA-R) via its PDZ domain, and is involved in their clustering. Moreover, it interacts with signaling molecules and plays an important role in coupling NMDA-R to pathways that control synaptic plasticity and learning. We found that PSD-95 is associated with the adenomatous polyposis coli (APC) tumor suppressor protein, Rap1-specific GAP (SPAL), LGN and tyrosine kinase Fyn. Our findings raise the possibility that these molecules are involved in the regulation of NMDA-R clustering and/or NMDA-R-mediated signal transduction.
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