Abstract
Pellino 3b Negatively Regulates Interleukin-1-induced TAK1-dependent NFκB Activation
Highlights
14654 JOURNAL OF BIOLOGICAL CHEMISTRY ing to hyperphosphorylation of IL-1 receptor-associated kinase (IRAK) [10], which creates an interface for its interaction with adapter Pellino 1 [11]
To examine whether IL-1-induced polyubiquitination of IRAK is linked via Lys-63 or Lys-48, HA-tagged wild type and a series of mutants of ubiquitin were transfected into 293 cells
Following in vitro ubiquitination assay, 20 l of Laemmli buffer was added into 10 l of reaction. 15 l of the reaction mixture was analyzed by Western blotting (WB) with anti-ubiquitin, and the other half was visualized by Coomassie Blue staining after resolving by 10% SDS-PAGE
Summary
14654 JOURNAL OF BIOLOGICAL CHEMISTRY ing to hyperphosphorylation of IRAK [10], which creates an interface for its interaction with adapter Pellino 1 [11]. Pellino 3b failed to inhibit found that IL-1-induced TAK1 modification and IB␣ degra- TNF␣-induced IB␣ phosphorylation, IB␣ degradation, or dation were reduced in Pellino 2 knockdown cells, suggesting JNK activation (Fig. 8E), indicating the specific role of Pellino the importance of Pellino 2 in TAK1-dependent NFB activa- 3b in regulating IL-1 signaling.
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