Apoptotic Activity of REAPER Is Distinct from Signaling by the Tumor Necrosis Factor Receptor 1 Death Domain*
- From the Department of Cell Biology and Neuroscience, University of Texas Southwestern Medical Center, Dallas, Texas 75235-9039
Abstract
REAPER (RPR) is a 65-amino acid protein that is critical activator of programmed cell death in Drosophila. On the basis of sequence alignment data, it was recently proposed that RPR might represent an ancestral molecule from which the death domain in a number of proteins may have evolved. We tested this idea by examining the activity of mutations in RPR that parallel inactivation mutations of the tumor necrosis factor receptor 1 death domain. The RPR mutants retained potent apoptotic function, suggesting that cell death activity mediated by RPR is distinct from signaling by the tumor necrosis factor receptor 1 death domain.
Footnotes
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↵* This work was supported by Grant AG12466 from the National Institutes of Health (to J. M. A.). 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.
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↵1 The abbreviations used are:
- TNFR
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tumor necrosis factor receptor
- HA
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hemagglutanmin
- hTNFR
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human TNFR.
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- Received May 17, 1996.
- Revision received August 23, 1996.
- © 1996 by The American Society for Biochemistry and Molecular Biology, Inc.
