The p53 tumor suppressor gene plays an instrumental role in transcriptional regulation of target genes involved in cellular stress responses. p53-dependent transactivation and transrepression require its interaction with p300/CBP, a coactivator that also interacts with the ReIA subunit of nuclear factor-κB. We find that p53 inhibits RelA-dependent transactivation without altering ReIA expression or inducible κB-DNA binding. p53-mediated repression of RelA is relieved by p300 overexpression and the increased RelA activity conferred by p53-deficiency is counteracted by either transactivation domain-deficient p300 fragments that bind RelA or a transdominant mutant of IκBα. Our results suggest that p53 can regulate diverse κB-dependent cellular responses.
Ravi, R., Mookerjee, B., van Hensbergen, Y., Bedi, G.C., Giordano, A., El-Deiry, W.S., et al. (1998). p53-mediated repression of nuclear factor-kappaB RelA via the transcriptional integrator p300. CANCER RESEARCH, 58(20), 4531-4536.
p53-mediated repression of nuclear factor-kappaB RelA via the transcriptional integrator p300
Giordano A.;
1998-01-01
Abstract
The p53 tumor suppressor gene plays an instrumental role in transcriptional regulation of target genes involved in cellular stress responses. p53-dependent transactivation and transrepression require its interaction with p300/CBP, a coactivator that also interacts with the ReIA subunit of nuclear factor-κB. We find that p53 inhibits RelA-dependent transactivation without altering ReIA expression or inducible κB-DNA binding. p53-mediated repression of RelA is relieved by p300 overexpression and the increased RelA activity conferred by p53-deficiency is counteracted by either transactivation domain-deficient p300 fragments that bind RelA or a transdominant mutant of IκBα. Our results suggest that p53 can regulate diverse κB-dependent cellular responses.I documenti in IRIS sono protetti da copyright e tutti i diritti sono riservati, salvo diversa indicazione.
https://hdl.handle.net/11365/35367
Attenzione
Attenzione! I dati visualizzati non sono stati sottoposti a validazione da parte dell'ateneo