The Journal of Experimental Medicine
Janeway's Immunobiology 7th Edition
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Published online 28 June 2004 doi:10.1084/jem.20040196
Rockefeller University Press, 0022-1007 $8.00
JEM, Volume 200, Number 1, 107-113
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Brief Definitive Report

 Degradation of Promoter-bound p65/RelA Is Essential for the Prompt Termination of the Nuclear Factor {kappa}B Response

Simona Saccani1, Ivan Marazzi1, Amer A. Beg2, and Gioacchino Natoli1

1 Institute for Research in Biomedicine, 6500 Bellinzona, Switzerland
2 Department of Biological Sciences, Columbia University, New York, NY 10027

Address correspondence to Gioacchino Natoli, Institute for Research in Biomedicine, Via Vela 6, 6500 Bellinzona, Switzerland. Phone: 41-91-8200-318; Fax: 41-91-8200-305; email: gioacchino.natoli{at}irb.unisi.ch

Transcription factors of the nuclear factor (NF)-{kappa}B/Rel family translocate into the nucleus upon degradation of the I{kappa}Bs. Postinduction repression of NF-{kappa}B activity depends on NF-{kappa}B–regulated resynthesis of I{kappa}B{alpha}, which dissociates NF-{kappa}B 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-{kappa}B is not promptly removed from some target genes in spite of I{kappa}B{alpha} 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.

Key Words: NF-{kappa}B • Rel family • proteasome • transcriptional regulation


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