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J. Biol. Chem., Vol. 275, Issue 35, 27084-27093, September 1, 2000
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From the Division of Biology, MC 156-29, Pasadena, California 91125
The caspase family of cysteine proteases plays
important roles in bringing about apoptotic cell death. All caspases
studied to date cleave substrates COOH-terminal to an aspartate. Here we show that the Drosophila caspase DRONC cleaves
COOH-terminal to glutamate as well as aspartate. DRONC autoprocesses
itself following a glutamate residue, but processes a second caspase, drICE, following an aspartate. DRONC prefers tetrapeptide substrates in
which aliphatic amino acids are present at the P2 position, and the P1
residue can be either aspartate or glutamate. Expression of a dominant
negative form of DRONC blocks cell death induced by the
Drosophila cell death activators reaper,
hid, and grim, and DRONC overexpression in
flies promotes cell death. Furthermore, the Drosophila cell
death inhibitor DIAP1 inhibits DRONC activity in yeast, and DIAP1's
ability to inhibit DRONC-dependent yeast cell death is
suppressed by HID and GRIM. These observations suggest that DRONC acts
to promote cell death. However, DRONC activity is not suppressed by the
caspase inhibitor and cell death suppressor baculovirus p35. We discuss
possible models for DRONC function as a cell death inhibitor.
The Drosophila Caspase DRONC Cleaves following
Glutamate or Aspartate and Is Regulated by DIAP1, HID, and GRIM*
§,¶,
,
*
This work was supported in part by grants from the Burroughs
Wellcome Fund (New Investigator awards in the Pharmacological Sciences), the Ellison Medical Foundation, and National Institutes of
Health Grant GM057422-01 (to B. A. H.).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.
Contributed equally to the results of this work.
§
Supported by a Human Frontiers postdoctoral fellowship. Current
address: Dept. of Haematology and Oncology, Royal Children's Hospital,
Flemington Road, Parkville, VIC 3052, Australia.
¶
Supported by a Jane Coffin Child postdoctoral fellowship.
Current address: Dept. of Enzymology, Merck Research
Laboratories, Rahway, NJ 07065.
**
Searle Scholar. To whom correspondence should be addressed. Tel.:
626-395-3399: Fax: 626-449-0756; E-mail: haybruce@its.
caltech.edu.
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