4.3 Article

The mammalian RNA-binding protein Staufen2 links nuclear and cytoplasmic RNA processing pathways in neurons

Journal

NEUROMOLECULAR MEDICINE
Volume 6, Issue 2-3, Pages 127-144

Publisher

HUMANA PRESS INC
DOI: 10.1385/NMM:6:2-3:127

Keywords

Staufen; nuclear pore protein; p62; tap; Y14; Mago; RNA transport; RNA export; RNA processing; NMD; EJC

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Members. of the Staufen family of RNA-binding proteins are highly conserved cytoplasmic RNA transporters associated with RNA granules. staufen2 is specifically expressed in neurons where the delivery of RNA to dendrites is thought to have a role in plasticity. We found that Staufen2 interacts with the nuclear pore protein p62, with the RNA export protein Tap and with the exon-exon junction complex (EJC) proteins Y14-Mago. The interaction of Staufen2 with the Y14-Mago heterodimer seems to represent a highly conserved complex as the same proteins are involved in the Staufen-mediated localization of oskar mRNA in Drosophila oocytes. A pool of Staufen2 is present in neuronal nuclei and colocalizes to a large degree with p62 and partly with Tap, Y14, and Mago. We suggest a model whereby a set of conserved genes in the oskar mRNA export pathway may be recruited to direct a dendritic destination for mRNAs originating as a Staufen2 nuclear complex.

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