Acetylation of MEK2 and I kappa B kinase (IKK) activation loop residues by YopJ inhibits signaling.

ABSTRACT: To overcome host defenses, bacterial pathogens of the genus Yersinia inject specific effector proteins into colonized mammalian cells. One such virulence factor, YopJ, inhibits the host inflammatory response and induces apoptosis of immune cells by blocking multiple signaling pathways, including the MAPK and NF-kappaB pathways. In this study, we show that YopJ exerts its deleterious effects by catalyzing the acetylation of two serine residues in the activation loop of the MAP kinase kinase, MEK2. This covalent modification prevents the phosphorylation of these serine residues that is required for activation of MEK2 and downstream signal propagation. We also show that YopJ causes acetylation of a threonine residue in the activation loop of both the alpha and beta subunits of the NF-kappaB p

SUBMITTER: Mittal R 

PROVIDER: S-EPMC1654131 | biostudies-literature | 2006 Dec

REPOSITORIES: biostudies-literature