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Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
 

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Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains.

Vertebrate tRNA export receptor exportin-t (Xpo-t) binds to RanGTP and mature tRNAs cooperatively to form a nuclear export complex. Xpo-t shuttles bidirectionally through nuclear pore complexes (NPCs) but is mainly nuclear at steady state. The steady-state distribution of Xpo-t is shown to depend on its interaction with RanGTP. Two distinct Xpo-t NPC interaction domains that bind differentially to peripherally localized nucleoporins in vitro are identified. The N terminus binds to both Nup153 and RanBP2/Nup358 in a RanGTP-dependent manner, while the C terminus binds to CAN/Nup214 independently of Ran. We propose that these interactions increase the concentration of tRNA export complexes and of empty Xpo-t in the vicinity of NPCs and thus increase the efficiency of the Xpo-t transport cycle.[1]

References

  1. Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains. Kuersten, S., Arts, G.J., Walther, T.C., Englmeier, L., Mattaj, I.W. Mol. Cell. Biol. (2002) [Pubmed]
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