Abstract
Nucleo-cytoplasmic transport comprises a large number of distinct pathways, many of which are defined by members of the importin beta superfamily of nuclear transport receptors. These transport receptors all directly interact with RanGTP to modulate the compartment-specific binding of their transport substrates. To identify new members of the importin beta family, we used affinity chromatography on immobilized RanGTP and isolated Ran-binding protein (RanBP) 16 from HeLa cell extracts. RanBP16 and its close human homologue, RanBP17, are distant members of the importin beta family. Like the other members of the transport receptor superfamily, RanBP16 interacts with the nuclear pore complex and is able to enter the nucleus independent of energy and additional nuclear transport receptors.
Highlights
Transport between the cytoplasm and the nucleus is largely mediated by members of the superfamily of importin -related nuclear transport receptors
Removal requires the concerted action of RanBP1 and the RanGTPaseactivating protein (RanGAP) that triggers the conversion of Ran into its GDP-bound form (11, 16 –18)
RanBP16 binds to the nuclear pore complex and, like all importin -related nuclear transport receptors, RanBP16 can enter the nucleus without the help of any other soluble factor
Summary
Transport between the cytoplasm and the nucleus is largely mediated by members of the superfamily of importin -related nuclear transport receptors (for review, see Refs. 1–3). To identify new members of the importin  family, we used affinity chromatography on immobilized RanGTP and isolated Ran-binding protein (RanBP) 16 from HeLa cell extracts.
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