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The Journal of Neuroscience, July 26, 2006, 26(30):7875-7884; doi:10.1523/JNEUROSCI.1851-06.2006

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Cellular/Molecular
Stargazin and Other Transmembrane AMPA Receptor Regulating Proteins Interact with Synaptic Scaffolding Protein MAGI-2 in Brain

Fang Deng, Maureen G. Price, Caleb F. Davis, Mayra Mori, and Daniel L. Burgess

Department of Neurology, Baylor College of Medicine, Houston, Texas 77030

Correspondence should be addressed to Dr. Daniel L. Burgess, Department of Neurology, Baylor College of Medicine, One Baylor Plaza, NB222, Houston, TX 77030. dburgess{at}bcm.tmc.edu

The spatial coordination of neurotransmitter receptors with other postsynaptic signaling and structural molecules is regulated by a diverse array of cell-specific scaffolding proteins. The synaptic trafficking of AMPA receptors by the stargazin protein in some neurons, for example, depends on specific interactions between the C terminus of stargazin and the PDZ [postsynaptic density-95 (PSD-95)/Discs large/zona occludens-1] domains of membrane-associated guanylate kinase scaffolding proteins PSD-93 or PSD-95. Stargazin [Cacng2 (Ca²⁺ channel 2 subunit)] is one of four closely related proteins recently categorized as transmembrane AMPA receptor regulating proteins (TARPs) that appear to share similar functions but exhibit distinct expression patterns in the CNS. We used yeast two-hybrid screening to identify MAGI-2 (membrane associated guanylate kinase, WW and PDZ domain containing 2) as a novel candidate interactor with the cytoplasmic C termini of the TARPs. MAGI-2 [also known as S-SCAM (synaptic scaffolding molecule)] is a multi-PDZ domain scaffolding protein that interacts with several different ligands in brain, including PTEN (phosphatase and tensin homolog), dasm1 (dendrite arborization and synapse maturation 1), dendrin, axin, - and -catenin, neuroligin, hyperpolarization-activated cation channels, 1-adrenergic receptors, and NMDA receptors. We confirmed that MAGI-2 coimmunoprecipitated with stargazin in vivo from mouse cerebral cortex and used in vitro assays to localize the interaction to the C-terminal -TTPV amino acid motif of stargazin and the PDZ1, PDZ3, and PDZ5 domains of MAGI-2. Expression of stargazin recruited MAGI-2 to cell membranes and cell–cell contact sites in transfected HEK-293T cells dependent on the presence of the stargazin -TTPV motif. These experiments identify MAGI-2 as a strong candidate for linking TARP/AMPA receptor complexes to a wide range of other postsynaptic molecules and pathways and advance our knowledge of protein interactions at mammalian CNS synapses.

Key words: stargazin; TARP; MAGI-2; S-SCAM; MAGUK; PDZ; AMPA

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Received May 1, 2006; revised June 14, 2006; accepted June 14, 2006.

Correspondence should be addressed to Dr. Daniel L. Burgess, Department of Neurology, Baylor College of Medicine, One Baylor Plaza, NB222, Houston, TX 77030. dburgess{at}bcm.tmc.edu

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				M. A. Bedoukian, J. D. Whitesell, E. J. Peterson, C. M. Clay, and K. M. Partin The Stargazin C Terminus Encodes an Intrinsic and Transferable Membrane Sorting Signal J. Biol. Chem., January 18, 2008; 283(3): 1597 - 1600. [Abstract] [Full Text] [PDF]

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