作者: Badal C. Roy , Kazuyoshi Kohu , Ken Matsuura , Hiroyuki Yanai , Tetsu Akiyama
DOI: 10.1046/J.1365-2443.2002.00546.X
关键词:
摘要: Background: The PSD-95 family of proteins possesses multiple protein binding domains, including three PDZ an SH3 domain, a HOOK domain and guanylate kinase-like (GK) domain. function as scaffolding that link ion channels such the N-methyl-d-aspartate-receptors (NMDA-Rs) with cytoskeletal networks signalling molecules, thereby controlling synaptic plasticity learning. Results: We found interact via their GK domains SPA-1-like (SPAL), GTPase-activating (GAP) is specific for Rap1. SPAL was contained within NMDA-R-PSD-95 complex, co-localized NMDA-R at synapses in cultured hippocampal neurones. Furthermore, NMDA stimulation induced dephosphorylation neurones. Conclusion: Our findings suggest may be involved NMDA-mediated organization signal transduction.