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 language | English |
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Pages (from-to) | 107-113 |
Number of pages | 7 |
Journal | Journal of Experimental Medicine |
Volume | 200 |
Issue number | 1 |
DOIs | |
Publication status | Published - Jul 5 2004 |
Keywords
- NF-κB
- Proteasome
- Rel family
- Transcriptional regulation
ASJC Scopus subject areas
- Immunology