3.1 Papers
3.1.6 Chronological list
3.1.6.59 Srivastava, S., Osten, P., Vilim, F.S.,Khatri, L., Inman, G., States, B., Daly, C., DeSouza, S., Abagyan, R., Valtschanoff, J.G., Weinberg, R.J. & Ziff, E.B. (1998). Novel Anchorage of GluR2/3 to the Postsynaptic Density by the AMPA Receptor-Binding Protein ABP. Neuron 21, 581-591
We report the cloning of -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.