Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor κB response

Simona Saccani, Ivan Marazzi, Amer A. Beg, Gioacchino Natoli

Research output: Contribution to journalArticle

Abstract

Transcription factors of the nuclear factor (NF)-κB/Rel family translocate into the nucleus upon degradation of the IκBs. Postinduction repression of NF-κB activity depends on NF-κB-regulated resynthesis of IκBα, which dissociates NF-κB from DNA and exports it to the cytosol. We found that after activation, p65/RelA is degraded by the proteasome in the nucleus and in a DNA binding-dependent manner. If proteasome activity is blocked, NF-κB is not promptly removed from some target genes in spite of IκBα resynthesis and sustained transcription occurs. These results indicate that proteasomal degradation of p65/RelA does not merely regulate its stability and abundance, but also actively promotes transcriptional termination.

Original languageEnglish
Pages (from-to)107-113
Number of pages7
JournalJournal of Experimental Medicine
Volume200
Issue number1
DOIs
Publication statusPublished - Jul 5 2004

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Proteasome Endopeptidase Complex
DNA
Cytosol
Transcription Factors
Genes

Keywords

  • NF-κB
  • Proteasome
  • Rel family
  • Transcriptional regulation

ASJC Scopus subject areas

  • Immunology

Cite this

Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor κB response. / Saccani, Simona; Marazzi, Ivan; Beg, Amer A.; Natoli, Gioacchino.

In: Journal of Experimental Medicine, Vol. 200, No. 1, 05.07.2004, p. 107-113.

Research output: Contribution to journalArticle

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