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J Biol Chem, Vol. 274, Issue 42, 29591-29594, October 15, 1999
-TrCP Mediates the Signal-induced Ubiquitination of
I
B
From the Section of Immunobiology and Department of Molecular
Biophysics and Biochemistry, Howard Hughes Medical Institute, Yale
University School of Medicine, New Haven, Connecticut 06520
We have examined the role of 
-TrCP
(-transducin repeat-containing protein) in the ubiquitination and
degradation of I
B, one of the two major IB isoforms in
mammalian cells. We demonstrate that -TrCP interacts specifically
with IB, and such interaction is dependent on prior
phosphorylation of IB on serines 19 and 23. Interaction with
-TrCP is also necessary for ubiquitination of IB upon
stimulation of cells, and deletion of the F-box in -TrCP abolishes
its ability to ubiquitinate IB. Therefore, these results indicate
that -TrCP plays a critical role in the activation of NF-B by
assembling the ubiquitin ligase complex for both phosphorylated
IB
and IB.
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