[HTML][HTML] The interleukin-1 receptor-associated kinase is degraded by proteasomes following its phosphorylation
TT Yamin, DK Miller - Journal of Biological Chemistry, 1997 - ASBMB
Following interleukin (IL)-1 stimulation, the majority of the cellular interleukin-1 receptor-
associated kinase (IRAK) translocates to a discrete subset of the Type I IL-1 receptor (IL-
1R1) in MRC-5 human lung fibroblasts. As the IRAK becomes multiphosphorylated, it is
degraded by proteasomes at a rate comparable to that of the degradation of the
phosphorylated IκBα protein. Proteasome inhibitors block the degradation of phosphorylated
IRAK and correspondingly increase the amount of IL-1R1 that can be coimmunoprecipitated …
associated kinase (IRAK) translocates to a discrete subset of the Type I IL-1 receptor (IL-
1R1) in MRC-5 human lung fibroblasts. As the IRAK becomes multiphosphorylated, it is
degraded by proteasomes at a rate comparable to that of the degradation of the
phosphorylated IκBα protein. Proteasome inhibitors block the degradation of phosphorylated
IRAK and correspondingly increase the amount of IL-1R1 that can be coimmunoprecipitated …
