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Mechanisms of NF-kB Activation and IkB Degradation via IKK Complex and Ubiquitination

This study explores the crucial role of the IKK kinase complex in the phosphorylation and subsequent ubiquitination of IkB, leading to its degradation by the 26S proteasome. The degradation of IkB releases NF-kB dimers, allowing their translocation into the nucleus and promoting gene expression. The interplay between various adaptor proteins and TNFα signaling in the cytoplasm underscores the complexity of this regulatory pathway. Figure 3 visually represents the key steps in NF-kB activation and IkB turnover.

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Mechanisms of NF-kB Activation and IkB Degradation via IKK Complex and Ubiquitination

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  1. Ub Ub Ub Ub Ub TNFa receptor cytoplasm adaptor proteins IKK kinase complex a b IKK complex NEMO IkB NF-kB 26S proteasome Phosphorylation of IkB Ubiquitination and degradation of IkB NF-kB ubiquitin Ub nucleus Gene expression phospho-serine Figure 3

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