IndraLab

Statements


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"We further demonstrated that Optn mediated recruitment of the deubiquitinase CYLD to TBK1 is responsible for this inhibitory effect."

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"As expected, formation of the TBK1 and CYLD complex was also reduced during the G2/M phase, while CYLD-Optn interaction remained unaffected as shown by co-immunoprecipitation and in situ PLA experiments performed in RO treated cells (Fig XREF_FIG, XREF_FIG and XREF_FIG, middle and lower panels, respectively)."

No evidence text available

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"CYLD also binds to TBK1 and CYLD -/- DCs show constitutive activation of TBK1."

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"Disruption of the interaction between TBK1 and CYLD should lead to higher ubiquitination levels of this kinase and consequently to its hyperactivation."

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"Disruption of the interaction between TBK1 and CYLD should lead to higher ubiquitination levels of this kinase and consequently to its hyperactivation."

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"Interestingly, the number of PLA specific dots observed using anti-TBK1 and anti-ubiquitin antibodies was increased in RO treated cells compared to untreated cells (XREF_FIG), strongly suggesting that disruption of the TBK1 and CYLD interaction during the G2/M transition led to increased ubiquitination of TBK1 and therefore to its activation [XREF_BIBR]."

No evidence text available

No evidence text available