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

doi:10.1016/S0896-6273(00)80568-1

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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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 language	English
Pages (from-to)	581-591
Number of pages	11
Journal	Neuron
Volume	21
Issue number	3
DOIs	https://doi.org/10.1016/S0896-6273(00)80568-1
Publication status	Published - 1998

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@article{c920b3df8b03434987a67fc6d6635538,

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

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.",

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

year = "1998",

doi = "10.1016/S0896-6273(00)80568-1",

language = "English",

volume = "21",

pages = "581--591",

journal = "Neuron",

issn = "0896-6273",

publisher = "Cell Press",

number = "3",

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TY - JOUR

T1 - Novel anchorage of GluR2/3 to the postsynaptic density by the AMPA receptor-binding protein ABP

AU - Srivastava, S

AU - Osten, P

AU - Vilim, F. S.

AU - Khatri, L

AU - Inman, G

AU - States, B

AU - Daly, C.

AU - DeSouza, S

AU - Abagyan, R

AU - Valtschanoff, J G

AU - Weinberg, R J

AU - Ziff, E B

PY - 1998

Y1 - 1998

N2 - 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.

AB - 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.

U2 - 10.1016/S0896-6273(00)80568-1

DO - 10.1016/S0896-6273(00)80568-1

M3 - Article

C2 - 9768844

SN - 0896-6273

VL - 21

SP - 581

EP - 591

JO - Neuron

JF - Neuron

IS - 3

ER -

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

Abstract

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