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J Biol Chem, Vol. 274, Issue 31, 21495-21498, July 30, 1999
B Kinases and Nuclear Factor B
Activities
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From the The adenovirus E1A protein has been implicated in
increasing cellular susceptibility to apoptosis induced by tumor
necrosis factor (TNF); however, its mechanism of action is still
unknown. Since activation of nuclear factor Section of Molecular Cell Biology, Department of Surgical Oncology, The University of Texas M. D. Anderson Cancer Center, Houston, Texas 77030
B (NF-B) has been
shown to play an anti-apoptotic role in TNF-induced apoptosis, we
examined apoptotic susceptibility and NF-B activation induced by
TNF in the E1A transfectants and their parental cells. Here, we
reported that E1A inhibited activation of NF-B and rendered cells
more sensitive to TNF-induced apoptosis. We further showed that this inhibition was through suppression of IB kinase (IKK) activity and
IB phosphorylation. Moreover, deletion of the p300 and Rb binding
domains of E1A abolished its function in blocking IKK activity and
IB phosphorylation, suggesting that these domains are essential for
the E1A function in down-regulating IKK activity and NF-B signaling.
However, the role of E1A in inhibiting IKK activity might be indirect.
Nevertheless, our results suggest that inhibition of IKK activity by
E1A is an important mechanism for the E1A-mediated sensitization of
TNF-induced apoptosis.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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