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
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