Journal article
The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID



Publication Details
Authors:
Wang, S.; Hawkins, C.; Yoo, S.; Müller, H.; Hay, B.
Publisher:
CELL PRESS
Publication year:
1999
Journal:
Cell
Pages range:
453-463
Volume number:
98
Issue number:
4
Start page:
453
End page:
463
Number of pages:
11
ISSN:
0092-8674

Abstract
Drosophila Reaper (RPR), Head Involution Defective (HID), and GRIM induce caspase-dependent cell death and physically interact with the cell death inhibitor DIAP1. Here we show that HID blocks DIAP1's ability to inhibit caspase activity and provide evidence suggesting that RPR and GRIM can act similarly. Based on these results, we propose that RPR, HID, and GRIM promote apoptosis by disrupting productive IAP-caspase interactions and that DIAP1 is required to block apoptosis-inducing caspase activity. Supporting this hypothesis, we show that elimination of DIAP1 function results in global early embryonic cell death and a large increase in DIAP1-inhibitable caspase activity and that DIAP1 is still required for cell survival when expression of rpr, hid, and grim is eliminated.


Authors/Editors

Last updated on 2019-25-07 at 19:33