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J. Biol. Chem., Vol. 278, Issue 6, 3590-3598, February 7, 2003

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The Proteoglycan NG2 Is Complexed with -Amino-3-hydroxy-5-methyl-4-isoxazolepropionic Acid (AMPA) Receptors by the PDZ Glutamate Receptor Interaction Protein (GRIP) in Glial Progenitor Cells
IMPLICATIONS FOR GLIAL-NEURONAL SIGNALING^*

Judith Stegmüller, Hauke Werner^§¶, Klaus-Armin Nave^§, and Jacqueline Trotter^**

From the  Department of Neurobiology, University of Heidelberg, Im Neuenheimer Feld 364, Heidelberg 69120, the  Unit of Molecular Cell Biology, Department of Zoology, University of Mainz, Bentzelweg 3, Mainz 55099, and the ^§ Max Planck Institute of Experimental Medicine, Hermann-Rein-Strasse 3, Göttingen 37075, Germany

The proteoglycan NG2 is expressed by immature glial cells in the developing and adult central nervous system. Using the COOH-terminal region of NG2 as bait in a yeast two-hybrid screen, we identified the glutamate receptor interaction protein GRIP1, a multi-PDZ domain protein, as an interacting partner. NG2 exhibits a PDZ binding motif at the extreme COOH terminus which binds to the seventh PDZ domain of GRIP1. In addition to the published expression in neurons, GRIP1 is expressed by immature glial cells. GRIP1 is known to bind to the GluRB subunit of the AMPA glutamate receptor expressed by subpopulations of neurons and immature glial cells. In cultures of primary oligodendrocytes, cells coexpress GluRB and NG2. A complex of NG2, GRIP1, and GluRB can be precipitated from transfected mammalian cells and from cultures of primary oligodendrocytes. Furthermore, NG2 and GRIP can be coprecipitated from developing brain tissue. These data suggest that GRIP1 acts as a scaffolding molecule clustering NG2 and AMPA receptors in immature glia. In view of the presence of synaptic contacts between neurons and NG2-positive glial cells in the hippocampus and the close association of NG2-expressing glial cells with axons, we suggest a role for the NG2·AMPA receptor complex in glial-neuronal recognition and signaling.

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