Importin beta -related receptors mediate translocation through nuclear pore
complexes. Co-operation with the RanGTPase system allows them to bind and
subsequently release their substrates on opposite sides of the nuclear enve
lope, which in turn ensures a directed nucleocytoplasmic transport. Here we
identify a novel family member from higher eukaryotes that functions prima
rily, but not exclusively, in import. It accounts for nuclear accumulation
of the SUMO-1/sentrin-conjugating enzyme hUBC9 and mediates import of the R
BM8 (Y14) protein, and is therefore referred to as importin 13 (Imp13). Une
xpectedly, Imp13 also shows export activity towards the translation initiat
ion factor eIF1A and is thus a case where a single importin beta -like rece
ptor transports different substrates in opposite directions. However, Imp13
operates differently from typical exportins in that the binding of eIF1A t
o Imp13 is only regulated indirectly by RanGTP, and the cytoplasmic release
of eIF1A from Imp13 is triggered by the loading of import substrates onto
Imp 13.