A nuclear export signal is essential for the cytosolic localization of the Ran binding protein, RanBP1

doi:10.1083/jcb.134.5.1157

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A nuclear export signal is essential for the cytosolic localization of the Ran binding protein, RanBP1

SA Richards, KM Lounsbury, KL Carey and IG Macara
Department of Pathology, University of Vermont, Burlington 05405-0068, USA. srichard@moose.uvm.edu

RanBP1 is a Ran/TC4 binding protein that can promote the interaction between Ran and beta-importin /beta-karyopherin, a component of the docking complex for nuclear protein cargo. This interaction occurs through a Ran binding domain (RBD). Here we show that RanBP1 is primarily cytoplasmic, but the isolated RBD accumulates in the nucleus. A region COOH-terminal to the RBD is responsible for this cytoplasmic localization. This domain acts heterologously, localizing a nuclear cyclin B1 mutant to the cytoplasm. The domain contains a nuclear export signal that is necessary but not sufficient for the nuclear export of a functional RBD In transiently transfected cells, epitope-tagged RanBP1 promotes dexamethasone-dependent nuclear accumulation of a glucocorticoid receptor-green fluorescent protein fusion, but the isolated RBD potently inhibits this accumulation. The cytosolic location of RanBP1 may therefore be important for nuclear protein import. RanBP1 may provide a key link between the nuclear import and export pathways.
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