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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
ACCELERATED PUBLICATION
I B Family Members Function by Different Mechanisms*
Winnie F.
Tam and
Ranjan
Sen
From the Rosenstiel Basic Medical Sciences Research Center and the
Department of Biology, Brandeis University, Waltham, Massachusetts
02454
The I B family of proteins regulates
NF- B-dependent transcription by inhibiting DNA binding
and localizing these factors to the cell cytoplasm. I B does this
by shifting the balance between nuclear import of Rel proteins and
their export from the nucleus. Here we show that, unlike I B ,
I B and I B appear to sequester p65 or c-Rel in the cytoplasm
by inhibiting nuclear import. Furthermore, because I B does not
undergo nucleocytoplasmic shuttling, it cannot remove nuclear proteins
like I B does. We conclude that the mechanism of action differs
among I 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.
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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Copyright © 2001 by the American Society for Biochemistry and Molecular Biology.
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