Interleukin-1 and TRAF6-dependent activation of TAK1 in the absence of TAB2 and TAB3

The Biochemical Journal
Jiazhen ZhangPhilip Cohen

Abstract

Interleukin-1 (IL-1) signaling induces the formation of Lys63-linked ubiquitin (K63-Ub) chains, which are thought to activate the 'master' protein kinase TGFβ-activated kinase 1 (TAK1) by interacting with its TAK1-binding 2 (TAB2) and TAB3 subunits. Here, we report that IL-1β can also activate the TAB1-TAK1 heterodimer present in TAB2/TAB3 double knockout (DKO) IL-1 receptor-expressing cells. The IL-1β-dependent activation of the TAB1-TAK1 heterodimer in TAB2/3 DKO cells is required for the expression and E3 ligase activity of tumor necrosis factor receptor-associated factor 6 (TRAF6) and is reduced by the small interfering RNA (siRNA) knockdown of ubiquitin conjugating 13 (Ubc13), an E2-conjugating enzyme that directs the formation of K63-Ub chains. IL-1β signaling was restored to TAB1/2/3 triple KO cells by the re-expression of either TAB1 or TAB2, but not by an ubiquitin binding-defective mutant of TAB2. We conclude that IL-1β can induce the activation of TAK1 in two ways, only one of which requires the binding of K63-Ub chains to TAB2/3. The early IL-1β-stimulated, TAK1-dependent activation of p38α mitogen-activated protein (MAP) kinase and the canonical IκB kinase (IKK) complex, as well as the NF-κB-dependent transcription...Continue Reading

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Citations

Jun 19, 2019·Proceedings of the National Academy of Sciences of the United States of America·Ian R KelsallPhilip Cohen
Apr 13, 2018·Biomedicines·Gilles Courtois, Marie-Odile Fauvarque
Jan 21, 2021·Frontiers in Immunology·Yan-Ran Xu, Cao-Qi Lei
Mar 13, 2021·Frontiers in Pharmacology·Hana MalcovaRudolf Horvath
Aug 31, 2021·European Journal of Human Genetics : EJHG·Aafke EngwerdaWilhelmina S Kerstjens-Frederikse
Jul 7, 2021·Journal of Cellular Biochemistry·Purushoth EthirajSakamuri V Reddy

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Methods Mentioned

BETA
restriction digests
PCRs
transfect
immunoprecipitation
transfection
PCR
ELISA

Software Mentioned

GraphPad Prism

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