Reptin physically interacts with p65 and represses NF-κB activation

FEBS Lett. 2015 Jul 8;589(15):1951-7. doi: 10.1016/j.febslet.2015.04.028. Epub 2015 May 6.

Abstract

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.

Keywords: Cytoplasma; NF-κB; Reptin; Transcription.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • ATPases Associated with Diverse Cellular Activities
  • Carrier Proteins / genetics
  • Carrier Proteins / metabolism*
  • Cell Line
  • DNA Helicases / genetics
  • DNA Helicases / metabolism*
  • Electrophoretic Mobility Shift Assay
  • Humans
  • Protein Binding
  • RNA Interference
  • RNA, Small Interfering / genetics
  • Transcription Factor RelA / metabolism*
  • Tumor Necrosis Factor-alpha / pharmacology

Substances

  • Carrier Proteins
  • RNA, Small Interfering
  • Transcription Factor RelA
  • Tumor Necrosis Factor-alpha
  • ATPases Associated with Diverse Cellular Activities
  • DNA Helicases
  • RUVBL2 protein, human