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

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.

journal_name

Mol Immunol

journal_title

Molecular immunology

authors

Kamal M,Valanciute A,Dahan K,Ory V,Pawlak A,Lang P,Guellaen G,Sahali D

doi

10.1016/j.molimm.2008.09.034

subject

Has Abstract

pub_date

2009-02-01 00:00:00

pages

991-8

issue

5

eissn

0161-5890

issn

1872-9142

pii

S0161-5890(08)00693-7

journal_volume

46

pub_type

杂志文章

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