IndraLab

Statements

TBK1 inhibits CYLD. 4 / 4
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"These data suggest that, in (CXCL4 + TLR8) costimulation, activation of TBK1 suppresses CYLD activation by phosphorylation, thereby reducing its cleavage by Caspase-8.RIPK1 kinase activity is regulated by TBK1 and Caspase-8 through direct phosphorylation at serine 320 and cleavage, respectively, while CYLD increases RIPK1 kinase activity by deubiquitylating K63 ubiquitin chain of RIPK1 [10, 15–17] (Fig. 1B)."
39715768
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"Furthermore, the activation of TBK1 is also negatively regulated by the phosphatases PPM1A (protein phosphatase magnesium dependent 1A), PPM1B, and PP4, as well as the deubiquitinating enzymes CYLD (cylindromatosis) and USP2b (ubiquitin specific protease 2b)."
30101190
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"However, inhibition of TBK1 activation by MRT67307 increased CYLD cleavage in (CXCL4 + TLR8) signaling (Fig. 1E)."
39715768
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"Because it was technically challenging to knockdown all four kinases of the IKK family simultaneously in a stable format, we resorted to using a dominant negative approach overexpressing a kinase-inactive TBK1, which could potentially block all the CYLD kinases."
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