0000000001222200

AUTHOR

Nadine Stöhr

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Activation of oligodendroglial Fyn kinase enhances translation of mRNAs transported in hnRNP A2-dependent RNA granules.

2008

Central nervous system myelination requires the synthesis of large amounts of myelin basic protein (MBP) at the axon–glia contact site. MBP messenger RNA (mRNA) is transported in RNA granules to oligodendroglial processes in a translationally silenced state. This process is regulated by the trans-acting factor heterogeneous nuclear ribonucleoprotein (hnRNP) A2 binding to the cis-acting A2 response element (A2RE). Release of this repression of MBP mRNA translation is thus essential for myelination. Mice deficient in the Src family tyrosine kinase Fyn are hypomyelinated and contain reduced levels of MBP. Here, we identify hnRNP A2 as a target of activated Fyn in oligodendrocytes. We show that…

Heterogeneous nuclear ribonucleoproteinCell Adhesion Molecules NeuronalRecombinant Fusion ProteinsBiologyHeterogeneous ribonucleoprotein particleCytoplasmic GranulesProto-Oncogene Proteins c-fynResponse Elementsenvironment and public healthRNA TransportCell LineMiceFYNContactinsGenes ReporterReportHeterogeneous-Nuclear Ribonucleoprotein Group A-BProtein biosynthesisAnimalsRNA MessengerPhosphorylationLuciferasesNeural Cell Adhesion MoleculesResearch ArticlesMessenger RNARNATranslation (biology)Cell BiologyMolecular biologyMyelin basic proteinEnzyme ActivationOligodendroglianervous systemProtein Biosynthesisbiology.proteinProtein BindingThe Journal of cell biology
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