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USP4 deubiquitinates MAP3K7. 13 / 13
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"USP4 deubiquitinates TAK1 in vitro and in vivo."

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"These results indicate that USP4 mainly inhibits inducible TAK1 polyubiquitination and activation whereas CYLD mainly inhibits basal level of TAK1 polyubiquitination and activation."

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"USP4 deubiquitinates TAK1 in vivo and in vitro."

"Using a functional genomic approach, we have identified ubiquitin-specific peptidase 4 (USP4) as a deubiquitinase for TAK1."

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"In addition, USP4 inhibits TNF-alpha-induced activation of NF-kappaB through USP4 deubiquitination of TAK1 XREF_BIBR."

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"Although it has been reported that USP4 deubiquitinates TAK1 and negatively regulates TNF- and IL-1-induced activation of NF-kappaB, how TAK1 ubiquitination is regulated in adaptive immune cells such as T cells and whether such a regulation regulates T cell mediated immune response remain unknown."

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"USP4 also deubiquitinates TAK1 in HEK293 T cells [62]."

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"In view of the data presented here and previous reports, we propose a working model (XREF_FIG), in which that TNFalpha rapidly induces Lys63 linked TAK1 polyubiquitnation and binding of USP4 to TAK1, Lys63 linked TAK1 would be rapidly deubiquitinated by USP4 to attenuate the magnitude of TNFalpha induced Lys63 linked TAK1 polyubiquitination and TAK1 mediated IKK and NF-kappaB activation."

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"We then analyzed the effect of USP4 knockdown on the TNFalpha induced TAK1 polyubiquitination."

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"In conclusion, our results provide evidence that TNFalpha induces association of USP4 with TAK1 which leads to TAK1 deubiquitination in the TNFalpha mediated NF-kappaB activation."

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"Mechanistically, p38IP dynamically interacts with TAK1 and promotes USP4 dependent deubiquitination of TAK1."

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"After TAK1 is activated with Lys63 linked polyubiquitination by Dox, USP4 deubiquitinates TAK1 and inhibits TAK1 mediated signaling."

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"Moreover, p38IP scaffolds the deubiquitinase USP4 to deubiquitinate TAK1 once TAK1 is activated."