High impact information on XPOT

• Yeast Los1p, the homolog of human exportin-t, mediates nuclear export of tRNA [1].
• Indeed, not only the canonical tRNA export receptor, exportin-t, but also Exp5 can drive nuclear export of tRNA [2].
• Exp5 thus represents the second directly RNA-binding exportin and mediates tRNA export in parallel with exportin-t. It was suggested recently that 10-15% of the cellular translation would occur in the nucleus [3].
• Steady-state nuclear localization of exportin-t involves RanGTP binding and two distinct nuclear pore complex interaction domains [4].
• The developmental defects caused by paused mutations confirm the important roles of exportin-t in gene expression in multicellular organisms [5].

Biological context of XPOT

• Vertebrate tRNA export receptor exportin-t (Xpo-t) binds to RanGTP and mature tRNAs cooperatively to form a nuclear export complex [4].
• The mutant phenotypes indicate that exportin-t acts pleiotropically in plant development [5].

Anatomical context of XPOT

• Thus, the present findings of decreased expression of exportin-1 and exportin-t induced by DVD can be correlated to inhibition of the proliferation of HL-60 cells [6].

Other interactions of XPOT

• Our results suggest further that vigilin and exportin-t might interact during tRNA export, provide evidence that the channeled tRNA cycle is already initiated in the nucleus, and illustrate that intracellular tRNA trafficking is associated with discrete changes in the composition of cellular cytoplasmic multi-protein complexes containing tRNA [7].

References