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Publication : Interaction of syntenin-1 and the NG2 proteoglycan in migratory oligodendrocyte precursor cells.

First Author  Chatterjee N Year  2008
Journal  J Biol Chem Volume  283
Issue  13 Pages  8310-7
PubMed ID  18218632 Mgi Jnum  J:135287
Mgi Id  MGI:3790944 Doi  10.1074/jbc.M706074200
Citation  Chatterjee N, et al. (2008) Interaction of syntenin-1 and the NG2 proteoglycan in migratory oligodendrocyte precursor cells. J Biol Chem 283(13):8310-7
abstractText  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.
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