PMC:3062687 / 23994-28180 JSONTXT

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The recent observation that human IKKβ displayed CK2-like phosphorylation specificity29 coincides with our evidence that recombinant IKKβ, but not IKKα, phosphorylated RPS3. We found this phosphorylation is a critical modulation for RPS3 nuclear translocation (via importin-α) and engagement in specific NF-κB transcription. CK2 was previously shown to phosphorylate p65 and to bind to and phosphorylate IKKβ41-43, however, we ruled out the possibility that the IKKβ-bound CK2 could account for the observed RPS3 phosphorylation because no CK2 was detected in the IKKβ preparations used for the in vitro kinase assay. Because RPS3 only harbors the CK2 motif and not a traditional IKK motif, this RPS3 regulatory function could explain why IKK harbors the alternative substrate phosphorylation capability.\nMore importantly, our study has elucidated how RPS3 is biochemically integrated into NF-κB activation signaling in a manner that is pivotal for the pathogenesis of foodborne pathogen E. coli O157:H7. IKKβ-mediated RPS3 S209 phosphorylation is a critical target modulated by this pathogen to subvert host NF-κB signaling. The bacterial effector NleH1 specifically binds to RPS3 once injected into host cells and profoundly suppresses NF-κB and its attendant protective immune responses9. Our data now show that NleH1 selectively inhibits RPS3 phosphorylation, thus retarding its nuclear translocation and subsequent NF-κB function, without altering other NF-κB signaling. Although NleH1 did not directly phosphorylate IKKβ, its kinase activity was required to inhibit IKKβ-mediated RPS3 S209 phosphorylation. Many bacteria pathogens have products that target key kinases to inactivate them in host cells, whereas E. coli O157:H7 employed NleH1 to steer the substrate specificity of IKKβ thus specifically fine-tuning host NF-κB signaling. This could represent a novel strategy to fine-tune host NF-κB signaling that could be shared by other pathogens. These data provide new insights into the poorly understood action mechanism for most T3SS effectors.\nNleH1 attenuates the transcription of RPS3-dependent, but not all, NF-κB target genes, in particular those genes associated with acute proinflammatory responses, including IL8 and TNF. In contrast, NleH1 does not block NF-κB p65 nuclear translocation, which suggests that certain p65-dependent but RPS3-independent NF-κB target genes might thus be beneficial for E. coli O157:H7 to replicate and disseminate in the host. By selectively inhibiting RPS3 and its attendant NF-κB function with NleH1, the pathogen achieves the ability to increase colonization and diarrhea yet limiting the mortality of the host. This seemingly paradoxical combination of effects make sense when one considers that increased bacterial load and diarrhea together with survival of the infected host would promote the spreading of the bacteria among a population of susceptible individuals. Such complex and paradoxical pathological effects that influence the spread of disease are often poorly understood at the molecular level. Our data elucidate how alterations in selective NF-κB function, achieved by impeding RPS3, but not altering p65 nuclear translocation, can influence specific cytokines that affect bacterial colonization, diarrhea diseases and mortality. It may be fruitful in attempting to understand other infectious and autoimmune diseases involving NF-κB to consider selective effects of subunits such as RPS3 in addition to global NF-κB 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