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 |
|---|---|
| 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 |
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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 journal › Article
}
TY - JOUR
T1 - Degradation of promoter-bound p65/RelA is essential for the prompt termination of the nuclear factor κB response
AU - Saccani, Simona
AU - Marazzi, Ivan
AU - Beg, Amer A.
AU - Natoli, Gioacchino
PY - 2004/7/5
Y1 - 2004/7/5
N2 - 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.
AB - 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.
KW - NF-κB
KW - Proteasome
KW - Rel family
KW - Transcriptional regulation
UR - http://www.scopus.com/inward/record.url?scp=3142771914&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=3142771914&partnerID=8YFLogxK
U2 - 10.1084/jem.20040196
DO - 10.1084/jem.20040196
M3 - Article
C2 - 15226358
AN - SCOPUS:3142771914
VL - 200
SP - 107
EP - 113
JO - Journal of Experimental Medicine
JF - Journal of Experimental Medicine
SN - 0022-1007
IS - 1
ER -