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Vol. 8, Issue 12, 2379-2390, December 1997
Department of Cell Biology, The Scripps Research Institute, La
Jolla, California 92037
RanBP2, a protein containing FG repeat motifs and four binding
sites for the guanosine triphosphatase Ran, is localized at the
cytoplasmic periphery of the nuclear pore complex (NPC) and is believed
to play a critical role in nuclear protein import. We purified RanBP2
from rat liver nuclear envelopes and examined its structural and
biochemical properties. Electron microscopy showed that RanBP2 forms a
flexible filamentous molecule with a length of ~36 nm, suggesting
that it comprises a major portion of the cytoplasmic fibrils implicated
in initial binding of import substrates to the NPC. Using in vitro
assays, we characterized the ability of RanBP2 to bind p97, a cytosolic
factor implicated in the association of the nuclear localization signal
receptor with the NPC. We found that RanGTP promotes the binding of p97 to RanBP2, whereas it inhibits the binding of p97 to other FG repeat
nucleoporins. These data suggest that RanGTP acts to specifically target p97 to RanBP2, where p97 may support the binding of an nuclear
localization signal receptor/substrate complex to RanBP2 in an early
step of nuclear import.
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