Mammalian mitochondrial IAP binding proteins

Author(s): Vaux, DL; Silke, J;
Details: Publication Year 2003-05-09,Volume 304,Issue #3,Page 499-504
Journal Title: BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
Publication Type: Journal Article
Abstract: Four mitochondrial proteins have been identified that immunoprecipitate with the mammalian inhibitor of apoptosis (IAP) protein XIAP. Each of them interacts via a processed amino terminus that resembles those of the insect pro-apoptotic TAP binding proteins Grim, HID, Reaper, and Sickle. Two, Diablo/Smac and HrtA2/Omi, have been extensively characterized. Both Diablo and HtrA2 can bind to IAPs and promote apoptosis when over-expressed in transfected cells, but unlike the insect IAP antagonists, to date there is scant evidence that they are important regulators of apoptosis in more physiological circumstances. (C) 2003 Elsevier Science (USA). All rights reserved.
Publisher: ACADEMIC PRESS INC ELSEVIER SCIENCE
Keywords: SERINE-PROTEASE OMI/HTRA2; DROSOPHILA CASPASE DRONC; ANTI-APOPTOTIC ACTIVITY; PROGRAMMED CELL-DEATH; STRUCTURAL BASIS; BIR DOMAIN; BACULOVIRUS INHIBITOR; PROMOTES APOPTOSIS; DEFICIENT MICE; NMR STRUCTURE
Publisher's Version: https://doi.org/10.1016/S0006-291X(03)00622-3
Terms of Use/Rights Notice: Refer to copyright notice on published article.

Creation Date: 2003-05-09 12:00:00