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J. Biol. Chem., Vol. 283, Issue 13, 8310-8317, March 28, 2008

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Interaction of Syntenin-1 and the NG2 Proteoglycan in Migratory Oligodendrocyte Precursor Cells^*

Nivedita Chatterjee¹, Judith Stegmüller¹², Philipp Schätzle, Khalad Karram, Michael Koroll, Hauke B. Werner^¶, Klaus-Armin Nave^¶, and Jacqueline Trotter³

From the Molecular Cell Biology, Department of Biology, Johannes Gutenberg University of Mainz, 55128 Mainz, Germany, the Max Delbrück Center for Molecular Medicine, 13125 Berlin, Germany, and the ^¶Department of Neurogenetics, Max Planck Institute of Experimental Medicine, 37075 Göttingen, Germany

Migration of oligodendrocyte precursors along axons is a necessary prerequisite for myelination, but little is known about underlying mechanisms. NG2 is a large membrane proteoglycan implicated in oligodendrocyte migration. Here we show that a PDZ domain protein termed syntenin-1 interacts with NG2 and that syntenin-1 is necessary for normal rates of migration. The association of syntenin-1 with NG2, identified in a yeast two-hybrid screen, was confirmed by colocalization of both proteins within processes of oligodendroglial precursor cells and by coimmunoprecipitation from cell extracts. Syntenin-1 also colocalizes with NG2 in "co-capping" assays, demonstrating a lateral association of both proteins in live oligodendrocytes. RNA interference-mediated down-regulation of syntenin-1 in glial cells results in a significant reduction of migration in vitro, as does the presence of polyclonal antibody against NG2. Thus syntenin plays a role in the migration of oligodendroglial precursors, and we suggest that NG2-syntenin-1 interactions contribute to this.

Received for publication, July 24, 2007 , and in revised form, January 18, 2008.

^* This work was supported by the Gemeinnützige Hertie Stiftung, the Deutsche Forschungsgemeinschaft (Schwerpunkt Programmes Cell Polarity and Glia-Synapse), and the European Union FP6 (Signaling and Traffic). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this factg.

¹ Both authors contributed equally to this work.

² Present address: Max Planck Inst. of Experimental Medicine, 37075 Göttingen, Germany.

³ To whom correspondence should be addressed: Molecular Cell Biology, Dept. of Biology, Bentzelweg 3, Johannes Gutenberg University of Mainz, 55128 Mainz, Germany. Tel.: 49-6131-3920263; Fax: 49-6131-3923840; E-mail: trotter{at}uni-mainz.de.

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				J. M. Beekman and P. J. Coffer The ins and outs of syntenin, a multifunctional intracellular adaptor protein J. Cell Sci., May 1, 2008; 121(9): 1349 - 1355. [Abstract] [Full Text] [PDF]