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Cell signalling

The NEMO guide to IκB

Nature Reviews Molecular Cell Biology volume 13, pages 408–409 (2012)Cite this article

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NEMO recognizes and binds to polyubiquitin chains on signalling molecules following stimulation, and this facilitates the activation of IKKβ by upstream kinases. Activated IKKβ phosphorylates ΙκBα, thereby promoting its degradation and the nuclear translocation of canonical NF-κB. In addition, activated IKKβ can phosphorylate other substrates, such as the p65 subunit of NF-κB (also known as RELA). Here, the authors report that, although the kinetics of IκBα and p65 phosphorylation by IKKβ differ in vivo (with IκBα being phosphorylated faster), active IKKβ processes these substrates with comparable kinetics in vitro. This suggests that a regulator may direct IKKβ activity towards IκBα in stimulated cells.

Interestingly, the ability of constitutively active IKKβ to promote IκBα phosphorylation and nuclear translocation of NF-κB in unstimulated fibroblasts depended on the presence of NEMO. As in vitro kinase assays showed that NEMO does not modify the catalytic activity of active IKKβ, the authors hypothesized that, in addition to its effects on IKKβ activation, NEMO acts downstream of active IKKβ to promote IκΒα phosphorylation.

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ORIGINAL RESEARCH PAPER

  1. Schröfelbauer, B. et al. NEMO ensures signaling specificity of the pleiotropic IKKβ by directing kinase activity toward IκBα. Mol. Cell 24 May 2012 (doi: 10.1016/j.molcel.2012.04.020)

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  1. Maria Papatriantafyllou
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Papatriantafyllou, M. The NEMO guide to IκB. Nat Rev Mol Cell Biol 13, 408–409 (2012). https://doi.org/10.1038/nrm3380

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