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Mol Immunol. 2009 Feb;46(5):991-8. doi: 10.1016/j.molimm.2008.09.034. Epub 2008 Nov 18.

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

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  • 1INSERM, U 841, Créteil 94010, France; Institut Mondor de Recherche Biomédicale (IMRB), Département "génétique", Equipe "21", Créteil, F-94010, France.


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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