Functional Analysis of the NMDA-recepter-APC-DLG-Complex.

突触蛋白PSD95/SAP90通过其PDZ结构域与N-甲基-D-天冬氨酸受体(NMDA-R)等离子通道相互作用，并参与它们的聚集。此外，它还与信号分子相互作用，并在将NMDA-R偶联到控制突触可塑性和学习的途径中发挥重要作用。我们发现PSD-95与结肠腺瘤性息肉病(APC)肿瘤抑制蛋白、RAP1特异性GAP(SPAL)、LGN和酪氨酸激酶Fyn相关。我们的发现提出了这些分子参与调控NMDA-R聚集和/或NMDA-R介导的信号转导的可能性。

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.