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Originally published In Press as doi:10.1074/jbc.M203464200 on October 22, 2002

J. Biol. Chem., Vol. 277, Issue 51, 49644-49650, December 20, 2002
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The Drosophila DIAP1 Protein Is Required to Prevent Accumulation of a Continuously Generated, Processed Form of the Apical Caspase DRONC*

Israel MuroDagger §, Bruce A. Hay, and Rollie J. ClemDagger ||

From the Dagger  Molecular, Cellular, and Developmental Biology Program, Division of Biology, Kansas State University, Manhattan, Kansas 66506 and  Division of Biology, MC156-29, California Institute of Technology, Pasadena, California 91125

Although loss of the inhibitor of apoptosis (IAP) protein DIAP1 has been shown to result in caspase activation and spontaneous cell death in Drosophila cells and embryos, the point at which DIAP1 normally functions to inhibit caspase activation is unknown. Depletion of the DIAP1 protein in Drosophila S2 cells or the Sf-IAP protein in Spodoptera frugiperda Sf21 cells by RNA interference (RNAi) or cycloheximide treatment resulted in rapid and widespread caspase-dependent apoptosis. Co-silencing of dronc or dark largely suppressed this apoptosis, indicating that DIAP1 is normally required to inhibit an activity dependent on these proteins. Silencing of dronc also inhibited DRICE processing following stimulation of apoptosis, demonstrating that DRONC functions as an apical caspase in S2 cells. Silencing of diap1 or treatment with UV light induced DRONC processing, which occurred in two steps. The first step appeared to occur continuously even in the absence of an apoptotic signal and to be dependent on DARK, because full-length DRONC accumulated when dark was silenced in non-apoptotic cells. In addition, treatment with the proteasome inhibitor MG132 resulted in accumulation of this initially processed form of DRONC, but not full-length DRONC, in non-apoptotic cells. The second step in DRONC processing was observed only in apoptotic cells. These results indicate that the initial step in DRONC processing occurs continuously via a DARK-dependent mechanism in Drosophila cells and that DIAP1 is required to prevent excess accumulation of this first form of processed DRONC, presumably through its ability to act as a ubiquitin-protein ligase.

* This work was supported in part by United States Public Health Service Grant CA78602 from the NCI, National Institutes of Health (to R. J. C.), and the Kansas Agricultural Experiment Station. This is Contribution Number 02-297-J from the Kansas Agricultural Experiment Station.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.

§ Recipient of support from NCI Predoctoral Training Grant T32 CA09418 from the National Institutes of Health.

|| To whom correspondence should be addressed: Division of Biology, 232 Ackert Hall, Kansas State University, Manhattan, KS 66506. Tel.: 785-532-3172; Fax: 785-532-6653; E-mail: rclem@ksu.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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