Reptin physically interacts with p65 and represses NF‐κB activation
Copyright policy )Reptin physically interacts with p65 and represses NF‐κB activation
Reptin and Pontin belong to the AAA+ ATPase family of DNA helicases. Both proteins are present in several chromatin‐remodeling machineries and are involved in transcriptional regulation, DNA repair, and telomerase activity, but they also function independently from each other. Here we report the identification of p65 as an interacting partner of Reptin. Using reporter gene assays, we show Reptin inhibits NF‐κB transactivation after TNFα stimulation. Reptin is mainly localized in the cytoplasm and impedes NF‐κB activation by inhibiting IκB‐α degradation and restraining p65 nuclear translocation. These results reveal a novel mechanism for the control of NF‐κB pathway by cytoplasmic Reptin.
- Guangxi University China (People's Republic of)
- Shanghai University of Traditional Chinese Medicine China (People's Republic of)
- Shanghai University China (People's Republic of)
- The First Affiliated Hospital of Guangxi University of Traditional Chinese Medicine China (People's Republic of)
Tumor Necrosis Factor-alpha, DNA Helicases, Transcription Factor RelA, Electrophoretic Mobility Shift Assay, Reptin, NF-κB, Cell Line, ATPases Associated with Diverse Cellular Activities, Humans, RNA Interference, Cytoplasma, RNA, Small Interfering, Carrier Proteins, Transcription, Protein Binding
Tumor Necrosis Factor-alpha, DNA Helicases, Transcription Factor RelA, Electrophoretic Mobility Shift Assay, Reptin, NF-κB, Cell Line, ATPases Associated with Diverse Cellular Activities, Humans, RNA Interference, Cytoplasma, RNA, Small Interfering, Carrier Proteins, Transcription, Protein Binding
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