Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor kappaB response.
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Saccani S, Marazzi I, Beg AA, Natoli G
Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor kappaB response.
J Exp Med. 2004 Jul 5;200(1):107-13. Epub 2004 Jun 28.
- PubMed ID
- 15226358 [ View in PubMed]
- Abstract
Transcription factors of the nuclear factor (NF)-kappaB/Rel family translocate into the nucleus upon degradation of the IkappaBs. Postinduction repression of NF-kappaB activity depends on NF-kappaB-regulated resynthesis of IkappaBalpha, which dissociates NF-kappaB 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-kappaB is not promptly removed from some target genes in spite of IkappaBalpha 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.