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Papers In Press, published online ahead of print January 10, 2001
J. Biol. Chem, 10.1074/jbc.C000916200
Submitted on December 22, 2000
Revised on January 10, 2001
Accepted on January 10, 2001

I-kappa B family members function by different mechanisms

Winnie F. Tam and Ranjan Sen

Biology, Brandeis University, Waltham, MA 02454

Corresponding Author: tam{at}brandeis.edu

The I-kappaB family of proteins regulates NF-kappaB dependent transcription by inhibiting DNA binding and localizing these factors to the cell cytoplasm. I-kappaB alpha does this by shifting the balance between nuclear import of Rel proteins and their export from the nucleus. Here we show that, unlike I-kappaB alpha, I-kappaB beta and I-kappaB epsilon appear to sequester p65, or c-Rel, in the cytoplasm by inhibiting nuclear import. Furthermore, because I-kappaB beta does not undergo nucleo-cytoplasmic shuttling, it cannot remove nuclear proteins like I-kappaB alpha does. We conclude that the mechanism of action of I-kappaB family members is different.


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