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Journal of Cell Science 115, 3285-3295 (2002)
© 2002 The Company of Biologists Limited

Research Article

Staufen2 isoforms localize to the somatodendritic domain of neurons and interact with different organelles

Thomas F. Duchaîne1,*, Indradeo Hemraj2,*, Luc Furic1, Anke Deitinghoff2, Michael A. Kiebler2 and Luc DesGroseillers1,3,{ddagger}

1 Department of Biochemistry, University of Montreal, Montreal, H3C 3J7, Canada
3 Centre de Recherches en Sciences Neurologiques, University of Montreal, Montreal, H3C 3J7, Canada
2 Max-Planck-Institute for Developmental Biology, Tübingen, Germany
* These authors contributed equally to this work

{ddagger} Author for correspondence (e-mail: luc.desgroseillers{at}umontreal.ca )

Accepted 5 June 2002

Mammalian Staufen2 (Stau2) is involved in mRNA transport in neurons. Here, we report that Stau2 is a double-stranded RNA-binding protein that is mainly expressed in the brain. We show that Stau2 is found in the somatodendritic compartment of neurons. In dendrites, Stau2 is aligned on individual tracts and colocalizes with microtubules. Stau2 is expressed as at least three splice isoforms, which can be observed in several subcellular complexes. Although a 62 kDa isoform (Stau262) fractionates in ribosome-free fractions of light density, Stau259 and Stau252 are found in high-density complexes. These complexes are resistant to EDTA and to non-ionic detergent. For the first time, we also provide evidence for an interaction of some Stau2 isoforms with ribosomes, thus pointing to an interesting new role for Stau2 in translation. EDTA treatment, which dissociates ribosome subunits, does not release Stau2 from the subunits, suggesting that Stau2-ribosome associations are not mediated mainly by mRNA intermediates. Although Stau2 has many features in common with its paralogue Stau1, it does not colocalize with Stau1-containing particles, indicating that these proteins are components of different complexes in dendrites. Our findings suggest that members of the Staufen family share evolutionarily conserved properties and highlight the complexity of Staufen-mediated RNA transport in neurons.

Key words: Staufen, Ribonucleoparticle, Ribosome, RNA-binding protein, RNA transport




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© The Company of Biologists Ltd 2002