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Volume 272, Number 27, Issue of July 4, 1997 pp. 16725-16728
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.

COMMUNICATION:
Activation of c-Jun N-terminal Kinase Antagonizes an Anti-apoptotic Action of Bcl-2

(Received for publication, February 28, 1997, and in revised form, May 2, 1997)

Jihyun Park , Injung Kim , Young Jun Oh ^§ , Ko-woon Lee ^¶ , Pyung-Lim Han ^¶ and Eui-Ju Choi

From the  Cell Biology and ^¶ Molecular Genetics Laboratories, Hanhyo Institute of Technology, 461-6, Jeonmin-dong, Yuseong-ku, Taejon 305-390, the  Graduate School of Biotechnology, Korea University, Seoul 136-701, and the ^§ Department of Biology, College of Science, Yonsei University, Seoul 120-749, Korea

Bcl-2 is an intracellular membrane-associated protein that prevents cell death induced by a variety of apoptotic stimuli. A mechanism by which Bcl-2 exerts an anti-cell death effect is, however, not fully understood. In the present study, Bcl-2 suppressed cell death of N18TG neuroglioma cells caused by various apoptotic stresses, including etoposide, staurosporine, anisomycin, and ultraviolet irradiation. Concomitantly, Bcl-2 disrupted a signaling cascade to the c-Jun N-terminal kinase activation induced by the apoptotic stresses. Bcl-2 also prevented the etoposide-induced stimulation of MEKK1. Furthermore, overexpression of c-Jun N-terminal kinase antagonized the death-protective function of Bcl-2. These data suggest that suppression of the c-Jun N-terminal kinase signaling pathway may be critical for Bcl-2 action.

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