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Originally published In Press as doi:10.1074/jbc.M011313200 on February 15, 2001

J. Biol. Chem., Vol. 276, Issue 19, 15840-15849, May 11, 2001
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Regulation of Nuclear Factor kappa B Transactivation
IMPLICATION OF PHOSPHATIDYLINOSITOL 3-KINASE AND PROTEIN KINASE C zeta  IN c-Rel ACTIVATION BY TUMOR NECROSIS FACTOR alpha *

Angel G. Martin, Belén San-Antonio, and Manuel FresnoDagger

From the Centro de Biología Molecular "Severo Ochoa," Universidad Autónoma de Madrid, Cantoblanco, Madrid 28049, Spain

Transactivation by c-Rel (nuclear factor kappa B) was dependent on phosphorylation of several serines in the transactivation domain, indicating that it is a phosphorylation-dependent Ser-rich domain. By Ser right-arrow Ala mutational and deletion analysis, we have identified two regions in this domain: 1) a C-terminal region (amino acids 540-588), which is required for basal activity; and 2) the 422-540 region, which responds to external stimuli as tumor necrosis factor (TNF) alpha  or phorbol myristate acetate plus ionomycin. Ser from 454 to 473 were shown to be required for TNFalpha -induced activation, whereas Ser between 492 and 519 were required for phorbol myristate acetate plus ionomycin activation. Phosphatidylinositol 3-kinase (PI3K) and protein kinase C (PKC) zeta  were identified as downstream signaling molecules of TNFalpha -activation of c-Rel transactivating activity. Interestingly, dominant negative forms of PI3K inhibited PKCzeta activation and dominant negative PKCzeta inhibited PI3K-mediated activation of c-Rel transactivating activity, indicating a cross-talk between both enzymes. We have identified the critical role of different Ser for PKCzeta - and PI3K-mediated responses. Interestingly, those c-Rel mutants not only did not respond to TNFalpha but also acted as dominant negative forms of nuclear factor kappa B activation.

* This work was supported by grants from Dirección General de Investigación Científica y Técnica, Fondo de Investigaciones Sanitarias, Comunidad Autónoma de Madrid, and Fundación Ramón Areces.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 34-913978413; Fax: 34-913974799; E-mail: mfresno@cbm.uam.es.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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