Literature DB >> 12059963

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

Badal C Roy1, Kazuyoshi Kohu, Ken Matsuura, Hiroyuki Yanai, Tetsu Akiyama.   

Abstract

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.

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Year:  2002        PMID: 12059963     DOI: 10.1046/j.1365-2443.2002.00546.x

Source DB:  PubMed          Journal:  Genes Cells        ISSN: 1356-9597            Impact factor:   1.891


  5 in total

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  5 in total

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