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XB-ART-14622
Mol Cell 1998 Feb 01;13:359-69.
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Identification of a tRNA-specific nuclear export receptor.

Kutay U , Lipowsky G , Izaurralde E , Bischoff FR , Schwarzmaier P , Hartmann E , Görlich D .


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In eukaryotes, tRNAs are synthesized in the nucleus and after several maturation steps exported to the cytoplasm. Here, we identify exportin-t as a specific mediator of tRNA export. It is a RanGTP-binding, importin beta-related factor with predominantly nuclear localization. It shuttles rapidly between nucleus and cytoplasm and interacts with nuclear pore complexes. Exportin-t binds tRNA directly and with high affinity. Its cellular concentration in Xenopus oocytes was found to be rate-limiting for export of all tRNAs tested, as judged by microinjection experiments. RanGTP regulates the substrate-exportin-t interaction such that tRNA can be preferentially bound in the nucleus and released in the cytoplasm.

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Species referenced: Xenopus
Genes referenced: kpnb1 mt-tr trna xpot