IndraLab

Statements

IKBKG binds KCNG1. 10 / 10
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"We and others have previously demonstrated that K13 interacts with NEMO and NEMO is essential for K13-induced NF-κB activation xref , xref ."
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"In a recent study, we demonstrated that TRAF2, which is required for NF-κB activation by TNFα, is not required for the interaction of K13 with NEMO and for K13-induced NF-κB activation xref ."
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"In this mechanism, K13 binds to the NEMO subunit, recruiting IKKα and IKKβ and consequent activation via phosphorylation [ xref ]."
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"However, the exact mechanism by which K13-NEMO interaction results in the activation of the IKK complex and the NF-κB pathway is not clear."
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"We further demonstrate that binding of K13 to NEMO is required for recruitment of IKK1 and IKK2 to K13."
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"We next asked the question how the interaction of K13 with NEMO results in the activation of the IKK complex and the NF-κB pathway."
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"Taken collectively, the above results support the model according to which binding of K13 to NEMO manipulates the latter into an open conformation that facilitates the recruitment of IKK1 and IKK2 and their subsequent activation by “T loop” phosphorylation."
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"However, it is not clear how K13-NEMO interaction results in the activation of the IKK complex."
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"Based on the lack of involvement of TRAF6, TAK1 and LUBAC in K13-induced NF-κB activation, we support a model according to which the interaction between K13 and NEMO is direct and is not mediated via the TRAF family members or the linear ubiquitin chains."
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"However, it has remained enigmatic how K13-NEMO interaction results in the activation of the IKK complex."
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