NF-κB essential modulator (NEMO), the non-catalytic regulatory subunit of the IκB kinase (IKK) complex, is
essential for the canonical NF-κB activation pathway. It has been identified as a molecular platform for assembling the
IKK complex and recruiting upstream IKK activators. However, the exact mechanism for regulating IKK activity has still
remained elusive. This review describes structural and functional characteristics of NEMO protein, covers the feasible
polyubiquitin-mediated NEMO-dependent IKK complex activation mechanism, and briefly summarizes some proteins
that bind to NEMO for enhancing or suppressing IKK complex activity. Furthermore, it also discusses several bioactive
compounds that disrupt the protein-protein interactions (PPI) involving NEMO, as these PPI may act as alternative routes
to develop novel pharmacological agents for inflammation and cancer therapy.
Keywords: IKKγ/NEMO, IKK activation model, K63-linked polyubiquitin chains, linear polyubiquitin chains, NEMO-binding
domain (NBD), oligomerzation states, protein-protein interactions.
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