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Reptin physically interacts with p65 and represses NF-κB activation.

Hua Qiu1, Yueqiu Gao2, Dewen Mao3

  • 1The First Affiliated Hospital of Guangxi University of Chinese Medicine, 89-9 Dongge Road, Nanning, Guangxi 530023, China; ShuGuang Hospital Affiliated to Shanghai University of Traditional Chinese Medicine, 528 Zhangheng Road, Pudong New Area, Shanghai 201203, China.

FEBS Letters
|May 10, 2015
PubMed
Summary

Reptin, a DNA helicase, interacts with p65 and inhibits the NF-κB pathway. Cytoplasmic Reptin prevents IκB-α degradation, blocking p65 nuclear translocation and NF-κB activation.

Keywords:
CytoplasmaNF-κBReptinTranscription

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Area of Science:

  • Molecular Biology
  • Cellular Biology
  • Biochemistry

Background:

  • Reptin and Pontin are AAA+ ATPase DNA helicases involved in chromatin remodeling, DNA repair, and transcriptional regulation.
  • These proteins participate in various cellular processes, often functioning independently.

Purpose of the Study:

  • To identify novel interacting partners of Reptin.
  • To elucidate the role of Reptin in the NF-κB signaling pathway.

Main Methods:

  • Co-immunoprecipitation to identify interacting partners.
  • Reporter gene assays to assess transcriptional activity.
  • Western blotting to analyze protein degradation and translocation.

Main Results:

  • p65 was identified as a novel interacting partner of Reptin.
  • Reptin inhibits NF-κB transactivation following TNFα stimulation.
  • Reptin localizes primarily in the cytoplasm and inhibits NF-κB activation by preventing IκB-α degradation and p65 nuclear translocation.

Conclusions:

  • Reptin acts as a negative regulator of the NF-κB signaling pathway.
  • Cytoplasmic localization of Reptin is crucial for its inhibitory function on NF-κB.
  • This study reveals a new mechanism controlling NF-κB pathway activation via Reptin.