IndraLab

Statements



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"We found that FK506 induces the degradation of both IkappaBalpha and IkappaBbeta and that the time courses of the FK506 induced degradation are quite different from degradation induced by interleukin 1 (IL-1)."

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"In the present study, we analyzed mechanisms by which FK506 induces IkappaBalpha degradation."

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"However, unlike IL-1-induced degradation, IKK-1 and IKK-2 were not activated significantly nor was FK506 induced IkappaBalpha degradation dependent on the N-terminal ubiquitination sites (Lys 21 and Lys 22)."

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"Despite this difference, FK506 induced IkappaBalpha degradation was dependent on the N-terminal Ser 32 and Ser 36 phosphorylation sites and was mediated by proteasomes, as is the case for IL-1-induced IkappaBalpha degradation."