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Originally published In Press as doi:10.1074/jbc.C000916200 on January 10, 2001

J. Biol. Chem., Vol. 276, Issue 11, 7701-7704, March 16, 2001
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ACCELERATED PUBLICATION
Ikappa B Family Members Function by Different Mechanisms*

Winnie F. Tam and Ranjan SenDagger

From the Rosenstiel Basic Medical Sciences Research Center and the Department of Biology, Brandeis University, Waltham, Massachusetts 02454

The Ikappa B family of proteins regulates NF-kappa B-dependent transcription by inhibiting DNA binding and localizing these factors to the cell cytoplasm. Ikappa Balpha does this by shifting the balance between nuclear import of Rel proteins and their export from the nucleus. Here we show that, unlike Ikappa Balpha , Ikappa Bbeta and Ikappa Bepsilon appear to sequester p65 or c-Rel in the cytoplasm by inhibiting nuclear import. Furthermore, because Ikappa Bbeta does not undergo nucleocytoplasmic shuttling, it cannot remove nuclear proteins like Ikappa Balpha does. We conclude that the mechanism of action differs among Ikappa B family members.


* 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.

Dagger To whom correspondence should be addressed: Rosenstiel Basic Medical Sciences Research Ctr., Brandeis University, 415 South St., Waltham, MA 02454. E-mail: sen@brandeis.edu.


Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.


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