C-mip interacts physically with RelA and inhibits nuclear factor kappa B activity

The fine regulation of NF-κB activity is crucial for both resting and stimulated cells and relies on complex balance between multiple activators and inhibitors. We report here that c-mip, a recently identified pleckstrin homology (PH) and leucine-rich repeat (LRR)-domain-containing protein, inactivates GSKβ and interacts with RelA, a key member of the NF-κB family. We show that c-mip inhibits the degradation of I-κBα and impedes the dissociation of the NF-κB/I-κBα complexes. C-mip acts downstream signaling of classical NF-κB pathway and may represent one of the missing links in the control of NF-κB activity.