PubMed:20976174 / 851-1737 JSONTXT

{"project":"PubMed_Structured_Abstracts","denotations":[{"id":"T2","span":{"begin":0,"end":886},"obj":"METHODS"}],"text":"Here, we performed an RNA interference (RNAi) screen on Shigella flexneri-induced NF-κB activation to identify new factors involved in the regulation of NF-κB following infection of epithelial cells by invasive bacteria. By targeting a subset of the human signaling proteome, we found that the catalytic subunit IKKα is also required for complete NF-κB activation during infection. Depletion of IKKα by RNAi strongly reduces the nuclear translocation of NF-κB p65 during S. flexneri infection as well as the expression of the proinflammatory chemokine interleukin-8. Similar to IKKβ, IKKα contributes to the phosphorylation of IκBα on serines 32 and 36, and to its degradation. Experiments performed with the synthetic Nod1 ligand L-Ala-D-γ-Glu-meso-diaminopimelic acid confirmed that IKKα is involved in NF-κB activation triggered downstream of Nod1-mediated peptidoglycan recognition."}

{"project":"Inflammaging","denotations":[{"id":"T7","span":{"begin":0,"end":220},"obj":"Sentence"},{"id":"T8","span":{"begin":221,"end":381},"obj":"Sentence"},{"id":"T9","span":{"begin":382,"end":566},"obj":"Sentence"},{"id":"T10","span":{"begin":567,"end":677},"obj":"Sentence"},{"id":"T11","span":{"begin":678,"end":886},"obj":"Sentence"},{"id":"T7","span":{"begin":0,"end":220},"obj":"Sentence"},{"id":"T8","span":{"begin":221,"end":381},"obj":"Sentence"},{"id":"T9","span":{"begin":382,"end":566},"obj":"Sentence"},{"id":"T10","span":{"begin":567,"end":677},"obj":"Sentence"},{"id":"T11","span":{"begin":678,"end":886},"obj":"Sentence"}],"text":"Here, we performed an RNA interference (RNAi) screen on Shigella flexneri-induced NF-κB activation to identify new factors involved in the regulation of NF-κB following infection of epithelial cells by invasive bacteria. By targeting a subset of the human signaling proteome, we found that the catalytic subunit IKKα is also required for complete NF-κB activation during infection. Depletion of IKKα by RNAi strongly reduces the nuclear translocation of NF-κB p65 during S. flexneri infection as well as the expression of the proinflammatory chemokine interleukin-8. Similar to IKKβ, IKKα contributes to the phosphorylation of IκBα on serines 32 and 36, and to its degradation. Experiments performed with the synthetic Nod1 ligand L-Ala-D-γ-Glu-meso-diaminopimelic acid confirmed that IKKα is involved in NF-κB activation triggered downstream of Nod1-mediated peptidoglycan recognition."}

{"project":"Allie","denotations":[{"id":"SS1_20976174_6_0","span":{"begin":22,"end":38},"obj":"expanded"},{"id":"SS2_20976174_6_0","span":{"begin":40,"end":44},"obj":"abbr"}],"relations":[{"id":"AE1_20976174_6_0","pred":"abbreviatedTo","subj":"SS1_20976174_6_0","obj":"SS2_20976174_6_0"}],"text":"Here, we performed an RNA interference (RNAi) screen on Shigella flexneri-induced NF-κB activation to identify new factors involved in the regulation of NF-κB following infection of epithelial cells by invasive bacteria. By targeting a subset of the human signaling proteome, we found that the catalytic subunit IKKα is also required for complete NF-κB activation during infection. Depletion of IKKα by RNAi strongly reduces the nuclear translocation of NF-κB p65 during S. flexneri infection as well as the expression of the proinflammatory chemokine interleukin-8. Similar to IKKβ, IKKα contributes to the phosphorylation of IκBα on serines 32 and 36, and to its degradation. Experiments performed with the synthetic Nod1 ligand L-Ala-D-γ-Glu-meso-diaminopimelic acid confirmed that IKKα is involved in NF-κB activation triggered downstream of Nod1-mediated peptidoglycan recognition."}