Jun 13, 2002

SPAL, a Rap-specific GTPase activating protein, is present in the NMDA receptor-PSD-95 complex in the hippocampus

Genes to Cells : Devoted to Molecular & Cellular Mechanisms
Badal C RoyTetsu Akiyama


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. 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. Our findings suggest that SPAL may be involved in the NMDA-mediated organization of cytoskeletal networks and signal transduction.

Mentioned in this Paper

Precipitin Tests
Protein Binding
Presynaptic density protein 95
Intracellular Signaling Proteins
RASA1 gene
Guanylate kinase
Ion Channel
DLG4 wt Allele

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