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TAK1 Lys-158 but not Lys-209 is required for IL-1β-induced Lys63-linked TAK1 polyubiquitination and IKK/NF-κB activation.

Abstract：

:The nuclear factor kappa B (NF-κB) transcription factor-mediated transcription is the endpoint of a series of signal transduction events that are initiated by a vast array of stimuli. Both the proteolytic and non-proteolytic functions of ubiquitination are critically important for the regulation of NF-κB activation. Lys63-linked polyubiquitination of TAK1 is required for IL-1β-induced IKK/NF-κB activation. However, the lysine site that mediates Lys63-linked TAK1 polyubiquitination in IL-1β signaling is still controversial. Here we report that TAK1 Lysine 158 but not Lysine 209 is required for IL-1β-induced Lys63-linked TAK1 polyubiquitination and TAK1-mediated IKK, JNK, and p38 activation. Co-overexpression of TAK1 wild-type and K209R mutant with TAB1 induced Lys63-linked TAK1 polyubiquitination and NF-κB activation whereas TAK1 K158R mutant failed to do so. Furthermore, IL-1β induces polyubiquitination of TAK1 wild-type and K209R mutant but not K158R mutant. Reconstitution of TAK1-deficient mouse embryo fibroblast cells with wild-type, K158R mutant, or K209R mutant TAK1 reveals that TAK1 Lys-158 but not Lys-209 is required for IL-1β-induced IKK, p38 and JNK activation.

journal_name

Cell Signal

journal_title

Cellular signalling

authors

Fan Y,Yu Y,Mao R,Zhang H,Yang J

doi

10.1016/j.cellsig.2010.11.017

subject

Has Abstract

pub_date

2011-04-01 00:00:00

pages

660-5

issue

4

eissn

0898-6568

issn

1873-3913

pii

S0898-6568(10)00343-8

journal_volume

23

pub_type

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