Novel anchorage of GluR2/3 to the postsynaptic density by the AMPA receptor-binding protein ABP

S Srivastava, P Osten, F. S. Vilim, L Khatri, G Inman, B States, C. Daly, S DeSouza, R Abagyan, J G Valtschanoff, R J Weinberg, E B Ziff

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    308 Citations (Scopus)

    Abstract

    We report the cloning of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionic acid (AMPA) receptor-binding protein (ABP), a postsynaptic density (PSD) protein related to glutamate receptor-interacting protein (GRIP) with two sets of three PDZ domains, which binds the GluR2/3 AMPA receptor subunits. ABP exhibits widespread CNS expression and is found at the postsynaptic membrane. We show that the protein interactions of the ABP/GRIP family differ from the PSD-95 family, which binds N-methyl-D-aspartate (NMDA) receptors. ABP binds to the GluR2/3 C-terminal VKI-COOH motif via class II hydrophobic PDZ interactions, distinct from the class I PSD-95-NMDA receptor interaction. ABP and GRIP also form homo- and heteromultimers through PDZ-PDZ interactions but do not bind PSD-95. We suggest that the ABP/GRIP and PSD-95 families form distinct scaffolds that anchor, respectively, AMPA and NMDA receptors.
    Original languageEnglish
    Pages (from-to)581-591
    Number of pages11
    JournalNeuron
    Volume21
    Issue number3
    DOIs
    Publication statusPublished - 1998

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