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MBC in Press, published online ahead of print November 18, 2002
Mol. Biol. Cell 10.1091/mbc.E02-07-0404

A more recent version of this article appeared on February 1, 2003
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Submitted on July 15, 2002
Revised on September 13, 2002
Accepted on October 21, 2002

I{kappa}B{alpha} and p65 regulate the cytoplasmic shuttling of Nuclear Corepressors: cross-talk between Notch and NF{kappa}B pathways

Lluís Espinosa1, Julia Inglés-Esteve1, Alex Robert-Moreno1, and Anna Bigas1*

1 Centre Oncologia Molecular, Institut de Recerca Oncologica, Hospitalet, Barcelona 08907, Spain

* Corresponding author. E-mail address: abigas{at}iro.es.

Notch and NF{kappa}B pathways are key regulators of numerous cellular events such as proliferation, differentiation, or apoptosis. In both pathways, association of effector proteins with nuclear corepressors is responsible for their negative regulation. We have previously described that expression of a p65-NF{kappa}B mutant that lacks the transactivation domain (p65{Delta}TA) induces cytoplasmic translocation of N-CoR leading to a positive regulation of different promoters. Now, we show that cytoplasmic sequestration of p65 by I{kappa}B{alpha} is sufficient to both translocate nuclear corepressors SMRT/N-CoR to the cytoplasm and upregulate transcription of Notch-dependent genes. Moreover, p65 and I{kappa}B{alpha} are able to directly bind SMRT and this interaction can be inhibited in a dose dependent manner by the CREB binding protein (CBP) coactivator and following TNF{alpha} treatment suggesting that p65 acetylation is modulating this interaction. In agreement with this, TNF{alpha} treatment results in downregulation of the Hes1 gene. Finally, we present evidence on how this mechanism may influence cell differentiation in the 32D myeloid progenitor system.




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