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J Biol Chem, Vol. 274, Issue 10, 6804-6812, March 5, 1999

Characterization of IB Nuclear Import Pathway

Pierre Turpin, Ronald T. Hay^¶, and Catherine Dargemont

From the  Laboratoire de Transport nucléocytoplasmique, Unité Mixte de Recherche 144 Institut Curie-CNRS, 26, rue d'Ulm, 75248 Paris Cedex 05, France and the ^¶ Institute of Biomolecular Sciences, School of Biomedical Sciences, University of St. Andrews, The North Haugh, St. Andrews, KY169TS, Scotland

IB controls the transcriptional activity of nuclear factor (NF)-B by retaining it in the cytoplasm; but, when expressed in the nucleus, it can also inhibit the interaction of NF-B with DNA and promote the export of NF-B from the nucleus to the cytoplasm. Here, we report that IB, when not bound to NF-B, is constitutively transported to the nucleus, and we confirm that the interaction of IB with NF-B retains IB in the cytoplasm. Nuclear import of IB does not result from passive diffusion but from a specific energy-dependent transport process that requires the ankyrin repeats of IB. Nuclear accumulation of IB is dependent on importins  and  as well as the small GTPase Ran, which are also responsible for the nuclear import mediated by basic nuclear localization sequences (NLS). However, these proteins are not sufficient to promote IB nuclear translocation. Factor(s) can be removed selectively from cell extracts with ankyrin repeats of IB which strongly reduce import of IB but not of proteins containing basic NLS. These findings indicate that IB is imported in the nucleus by a piggy-back mechanism that involves additional protein(s) containing a basic NLS and able to interact with ankyrin repeats of IB.

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Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.

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