2003
DOI: 10.1074/jbc.m304374200 View full text |Buy / Rent full text
|
|

Abstract: However, the events contributing to IKK␤ phosphorylation are not well understood. Here, we present evidence that the activation of IKK␤ depends on its ability to form homotypic interactions and to transautophosphorylate. We find that an intact leucine zipper in IKK␤ is necessary for homotypic interactions, kinase activation, and phosphorylation on its activation loop. Enforced oligomerization of an IKK␤ mutant defective in forming homotypic interactions restores kinase activation. Homotypic interactions allow … Show more

Help me understand this report

Search citation statements

Order By: Relevance
Select...
1
37
1

Publication Types

Select...

Relationship

0
0

Authors

Journals