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The Journal of Neuroscience, August 20, 2003, 23(20):7592-7601

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Intracellular Membrane Targeting and Suppression of Ser⁸⁸⁰ Phosphorylation of Glutamate Receptor 2 by the Linker I-Set II Domain of AMPA Receptor-Binding Protein

Jie Fu, Sunita deSouza, and Edward B. Ziff

Howard Hughes Medical Institute, Department of Biochemistry, New York University School of Medicine, New York, New York 10016

AMPA receptor-binding protein (ABP) is a multi-postsynaptic density-95/discs large/zona occludens (PDZ) protein that binds to the glutamate receptor 2/3 (GluR2/3) subunits of the AMPA receptor and is implicated in receptor membrane anchorage. A palmitoylated form of ABP localizes to spine heads, whereas a nonpalmitoylated form is found in intracellular clusters. Here, we investigate intracellular cluster formation by ABP and the ability of ABP to associate with GluR2 while in these clusters. We show that ABP interacts with intracellular membranes via the ABP linker I (LI)-set II (SII) subdomain, a region consisting of ABP linker 1 and PDZ4, -5, and -6. This suggests that cluster formation results from LI-SII ABP association with the membrane of a vesicular structure. We present evidence that ABP can self-associate at intracellular membrane surfaces via interactions involving SII. ABP in such membrane clusters can bind and retain GluR2 that has trafficked endocytotically from the plasma membrane. Phosphorylation of GluR2 at serine 880, proximal to the ABP binding site, has been implicated by others in the release of ABP from GluR2 and the mobilization of AMPA receptors for trafficking. We show that binding of GluR2 to ABP blocks phosphorylation of serine 880. This suggests that ABP can stabilize its own association with GluR2. We discuss a model in which ABP can form a protein scaffold at a vesicular membrane that is capable of binding GluR2, leading to formation of an intracellular AMPA receptor pool. Receptors in such a pool may contribute to receptor endocytotic and exocytotic trafficking and recycling.

Key words: AMPA receptors; ABP; GRIP; trafficking; endocytosis; PDZ domain; phosphorylation

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Received Feb. 28, 2003; revised Jun. 18, 2003; accepted Jun. 19, 2003.

This article has been cited by other articles:

				J. B. Silverman, S. Restituito, W. Lu, L. Lee-Edwards, L. Khatri, and E. B. Ziff Synaptic Anchorage of AMPA Receptors by Cadherins through Neural Plakophilin-Related Arm Protein AMPA Receptor-Binding Protein Complexes J. Neurosci., August 8, 2007; 27(32): 8505 - 8516. [Abstract] [Full Text] [PDF]

				S. Monea, B. A. Jordan, S. Srivastava, S. DeSouza, and E. B. Ziff Membrane localization of membrane type 5 matrix metalloproteinase by AMPA receptor binding protein and cleavage of cadherins. J. Neurosci., February 22, 2006; 26(8): 2300 - 2312. [Abstract] [Full Text] [PDF]

				C. L. Palmer, L. Cotton, and J. M. Henley The Molecular Pharmacology and Cell Biology of {alpha}-Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid Receptors Pharmacol. Rev., June 1, 2005; 57(2): 253 - 277. [Abstract] [Full Text] [PDF]

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