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Originally published In Press as doi:10.1074/jbc.M004751200 on August 31, 2000

J. Biol. Chem., Vol. 275, Issue 46, 36441-36449, November 17, 2000
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Ikappa Balpha and Ikappa Balpha /NF-kappa B Complexes Are Retained in the Cytoplasm through Interaction with a Novel Partner, RasGAP SH3-binding Protein 2*

Magali PrigentDagger , Isabelle Barlat§, Hanno Langen, and Catherine DargemontDagger ||

From the Dagger  Laboratoire de Transport Nucleocytoplasmique, Institut Curie-CNRS UMR144, 26 rue d'Ulm, 75248 Paris Cedex 05, France, § Avantis Pharma, 94403 Vitry s/Seine, France, and  F. Hoffmann-La Roche AG, PRPN-G, Building 93/440, 4070 Basel, Switzerland

Ikappa Balpha inhibits the transcriptional activity of NF-kappa B both in the cytoplasm by preventing the nuclear translocation of NF-kappa B and in the nucleus where it dissociates NF-kappa B from DNA and transports it back to the cytoplasm. Cytoplasmic localization of inactive NF-kappa B/Ikappa Balpha complexes is controlled by mutual masking of nuclear import sequences of NF-kappa B p65 and Ikappa Balpha and active CRM1-mediated nuclear export. Here, we describe an additional mechanism accounting for the cytoplasmic anchoring of Ikappa Balpha or NF-kappa B/Ikappa Balpha complexes. The N-terminal domain of Ikappa Balpha contains a sequence responsible for the cytoplasmic retention of Ikappa Balpha that is specifically recognized by G3BP2, a cytoplasmic protein that interacts with both Ikappa Balpha and Ikappa Balpha /NF-kappa B complexes. G3BP2 is composed of an N-terminal domain homologous to the NTF2 protein, followed by an acidic domain sufficient for the interaction with the Ikappa Balpha cytoplasmic retention sequence, a region containing five PXXP motifs and a C-terminal domain containing RNA-binding motifs. Overexpression of G3BP2 directly promotes retention of Ikappa Balpha in the cytoplasm, indicating that subcellular distribution of Ikappa Balpha and NF-kappa B/Ikappa Balpha complexes likely results from a equilibrium between nuclear import, nuclear export, and cytoplasmic retention. The molecular organization of G3BP2 suggests that this putative scaffold protein might connect the NF-kappa B signal transduction cascade with cellular functions such as nuclear transport or RNA metabolism.

* This work was supported in part by grants from the Association de Recherche contre le Cancer.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| To whom correspondence should be addressed: Laboratoire de Transport Nucleocytoplasmique, Institut Jacques Monod-CNRS UMR 7592, Tour 43, 2, Place Jussieu, 75251 Paris Cedex 05, France. Tel.: 33-1-44276956; Fax: 33-1-44276956; E-mail: dargemont@ijm.jussieu.fr.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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