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J Biol Chem, Vol. 275, Issue 20, 15193-15199, May 19, 2000

Inducible NF-B Activation Is Permitted by Simultaneous Degradation of Nuclear IB^*

Patricia Renard^§, Yann Percherancier^§, Mathias Kroll^¶, Dominique Thomas, Jean-Louis Virelizier, Fernando Arenzana-Seisdedos, and Françoise Bachelerie

From the Unité d'Immunologie Virale, Institut Pasteur, 28 rue du Dr. Roux, 75015 Paris, France

Signal-induced phosphorylation and ubiquitination of IB targets this inhibitor of NF-B for proteasome-mediated degradation, thus permitting the release of active NF-B. Upon cell stimulation, NF-B activation results in neotranscription and neosynthesis of its own inhibitor, IB. As reported earlier, the neosynthesized inhibitor is then accumulated in the nucleus, where it rapidly binds to and terminates the function of nuclear NF-B upon withdrawal of the stimulus. The present work was aimed at understanding how NF-B activity is preserved while stimuli persist, despite intense, simultaneous IB neosynthesis, which would be expected to end NF-B activity. We here show that incoming IB in the nucleus represents a target for resident nuclear proteasome complexes. Signal-induced, proteasome-dependent degradation of phosphorylated and ubiquitinated IB occurs in the nucleus, thus permitting the onset and persistence of NF-B activity as long as stimulation is maintained. Our results suggest that intranuclear proteolysis of IB is necessarily required to avoid self-termination of NF-B activity during cell activation.

This work was supported in part by grants from the Agence Nationale de la Recherche sur le Sida (ANRS, France), the Association pour la Recherche sur le Cancer (France), and the European Communities Concerted Action BIOMED II (ROCIO Project).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.

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