scholarly journals Unique BIR domain sets determine inhibitor of apoptosis protein–driven cell death and NOD2 complex signal specificity

2018 ◽  
Vol 11 (539) ◽  
pp. eaao3964 ◽  
Author(s):  
Steven M. Chirieleison ◽  
Joseph K. Rathkey ◽  
Derek W. Abbott
Keyword(s):  
Cell Death ◽  
Complex Signal ◽  
Inhibitor Of Apoptosis ◽  
Inhibitor Of Apoptosis Protein ◽  
Apoptosis Protein ◽  
Signal Specificity ◽  
Bir Domain

scholarly journals Pseudomonas aeruginosaDelays Kupffer Cell Death via Stabilization of the X-Chromosome-Linked Inhibitor of Apoptosis Protein

2007 ◽  
Vol 179 (1) ◽  
pp. 505-513 ◽  
Author(s):  
Alix Ashare ◽  
Martha M. Monick ◽  
Amanda B. Nymon ◽  
John M. Morrison ◽  
Matthew Noble ◽  
...  
Keyword(s):  
Cell Death ◽  
X Chromosome ◽  
Kupffer Cell ◽  
Inhibitor Of Apoptosis ◽  
Inhibitor Of Apoptosis Protein ◽  
Apoptosis Protein

scholarly journals Diablo Promotes Apoptosis by Removing Miha/Xiap from Processed Caspase 9

2001 ◽  
Vol 152 (3) ◽  
pp. 483-490 ◽  
Author(s):  
Paul G. Ekert ◽  
John Silke ◽  
Christine J. Hawkins ◽  
Anne M. Verhagen ◽  
David L. Vaux
Keyword(s):  
Cell Death ◽  
Cytochrome C ◽  
Caspase 3 ◽  
Direct Interaction ◽  
Inhibitor Of Apoptosis ◽  
Caspase 9 ◽  
Inhibitor Of Apoptosis Protein ◽  
Grim Reaper ◽  
Apoptosis Protein ◽  
Mammalian Protein

MIHA is an inhibitor of apoptosis protein (IAP) that can inhibit cell death by direct interaction with caspases, the effector proteases of apoptosis. DIABLO is a mammalian protein that can bind to IAPs and antagonize their antiapoptotic effect, a function analogous to that of the proapoptotic Drosophila molecules, Grim, Reaper, and HID. Here, we show that after UV radiation, MIHA prevented apoptosis by inhibiting caspase 9 and caspase 3 activation. Unlike Bcl-2, MIHA functioned after release of cytochrome c and DIABLO from the mitochondria and was able to bind to both processed caspase 9 and processed caspase 3 to prevent feedback activation of their zymogen forms. Once released into the cytosol, DIABLO bound to MIHA and disrupted its association with processed caspase 9, thereby allowing caspase 9 to activate caspase 3, resulting in apoptosis.

scholarly journals Neurotrophin Receptor-interacting Mage Homologue Is an Inducible Inhibitor of Apoptosis Protein-interacting Protein That Augments Cell Death

2001 ◽  
Vol 276 (43) ◽  
pp. 39985-39989 ◽  
Author(s):  
Bruce W. M. Jordan ◽  
Dragomir Dinev ◽  
Veronique LeMellay ◽  
Jakob Troppmair ◽  
Rudolf Götz ◽  
...  
Keyword(s):  
Cell Death ◽  
Neurotrophin Receptor ◽  
Inhibitor Of Apoptosis ◽  
Interacting Protein ◽  
Inhibitor Of Apoptosis Protein ◽  
Apoptosis Protein
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