| First Author | Roy BC | Year | 2002 |
| Journal | Genes Cells | Volume | 7 |
| Issue | 6 | Pages | 607-17 |
| PubMed ID | 12059963 | Mgi Jnum | J:113986 |
| Mgi Id | MGI:3687938 | Doi | 10.1046/j.1365-2443.2002.00546.x |
| Citation | Roy BC, et al. (2002) SPAL, a Rap-specific GTPase activating protein, is present in the NMDA receptor-PSD-95 complex in the hippocampus. Genes Cells 7(6):607-17 |
| abstractText | BACKGROUND: The PSD-95 family of proteins possesses multiple protein binding domains, including three PDZ domains, an SH3 domain, a HOOK domain and a guanylate kinase-like (GK) domain. The PSD-95 proteins function as scaffolding proteins that link ion channels such as the N-methyl-d-aspartate-receptors (NMDA-Rs) with cytoskeletal networks and signalling molecules, thereby controlling synaptic plasticity and learning. RESULTS: We found that the PSD-95 family proteins interact via their GK domains with SPA-1-like protein (SPAL), a GTPase-activating protein (GAP) that is specific for Rap1. SPAL was contained within the NMDA-R-PSD-95 complex, and co-localized with PSD-95 and NMDA-R at the synapses in cultured hippocampal neurones. Furthermore, NMDA stimulation induced the dephosphorylation of SPAL in cultured hippocampal neurones. CONCLUSION: Our findings suggest that SPAL may be involved in the NMDA-mediated organization of cytoskeletal networks and signal transduction. |
