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  • Title: C-mip interacts physically with RelA and inhibits nuclear factor kappa B activity.
    Author: Kamal M, Valanciute A, Dahan K, Ory V, Pawlak A, Lang P, Guellaen G, Sahali D.
    Journal: Mol Immunol; 2009 Feb; 46(5):991-8. PubMed ID: 19019440.
    Abstract:
    The fine regulation of NF-kappaB 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 GSKbeta and interacts with RelA, a key member of the NF-kappaB family. We show that c-mip inhibits the degradation of I-kappaBalpha and impedes the dissociation of the NF-kappaB/I-kappaBalpha complexes. C-mip acts downstream signaling of classical NF-kappaB pathway and may represent one of the missing links in the control of NF-kappaB activity.
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