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MBC in Press, published online ahead of print February 25, 2009
Mol. Biol. Cell 10.1091/mbc.E08-11-1151

A more recent version of this article appeared on April 15, 2009
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Submitted on November 26, 2008
Revised on February 10, 2009
Accepted on February 12, 2009

Nuclear Shuttling of She2p Couples ASH1 mRNA Localization to its Translational Repression by Recruiting Loc1p and Puf6p

Zhifa Shen, Nicolas Paquin,* Amélie Forget, and Pascal Chartrand*

Département de Biochimie, Université de Montréal, Montréal, Qc H3C 3J7 Canada

Monitoring Editor: Marvin P. Wickens

The transport and localization of mRNAs results in the asymmetric synthesis of specific proteins. In yeast, the nucleo-cytoplasmic shuttling protein She2 binds the ASH1 mRNA and targets it for localization at the bud tip by recruiting the She3p-Myo4p complex. While the cytoplasmic role of She2p in mRNA localization is well characterized, its nuclear function is still unclear. Here, we show that She2p contains a nonclassical nuclear localization signal (NLS) which is essential for its nuclear import via the importin {alpha} Srp1p. Exclusion of She2p from the nucleus by mutagenesis of its NLS leads to defective ASH1 mRNA localization and Ash1p sorting. Interestingly, these phenotypes mimic knockouts of LOC1 and PUF6, which encode for nuclear RNA-binding proteins that bind the ASH1 mRNA and control its translation. We find that She2p interacts with both Loc1p and Puf6p, and that excluding She2p from the nucleus decreases this interaction. Absence of nuclear She2p disrupts the binding of Loc1p and Puf6p to the ASH1 mRNA, suggesting that nuclear import of She2p is necessary to recruit both factors to the ASH1 transcript. This study reveals that a direct coupling between localization and translation regulation factors in the nucleus is required for proper cytoplasmic localization of mRNAs.

Address correspondence to:

*present address: Department of Biology, MIT, Cambridge, MA 02139 Pascal Chartrand (p.chartrand{at}umontreal.ca)




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