Cell death regulation by the mammalian IAP antagonist Diablo/Smac

Apoptosis

Volumn 7, Issue 2, 2002, Pages 163-166

  Verhagen, A M ^a   Vaux, D L ^a  

^a ROYAL MELBOURNE HOSPITAL   (Australia)

Author keywords

Apoptosis; Diablo; Grim; HID; IAP; Mitochondria; Reaper; Smac

Indexed keywords

CASPASE; CELL PROTEIN; INHIBITOR OF APOPTOSIS PROTEIN; SECOND MITOCHONDRIAL ACTIVATOR OF CASPASE; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CELL DEATH; DROSOPHILA; ENZYME INHIBITION; GENE LOCUS; MAMMAL CELL; NONHUMAN; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; TRANSCRIPTION REGULATION;

AMINO ACID SEQUENCE; ANIMALS; APOPTOSIS; CARRIER PROTEINS; CELL DEATH; DROSOPHILA; INTRACELLULAR SIGNALING PEPTIDES AND PROTEINS; MITOCHONDRIAL PROTEINS; MODELS, BIOLOGICAL; MOLECULAR SEQUENCE DATA; PEPTIDES; PROTEIN BINDING; PROTEIN STRUCTURE, TERTIARY; SEQUENCE HOMOLOGY, AMINO ACID; TRANSCRIPTION, GENETIC;

INTRACISTERNAL A-PARTICLES; MAMMALIA;

EID: 0036204018     PISSN: 13608185     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1014318615955     Document Type: Article

References (25)

1. Smac, a mitochondrial protein that promotes cytochrome c-dependent caspase activation by eliminating IAP inhibition
2. Identification of DIABLO, a mammalian protein that promotes apoptosis by binding to and antagonizing IAP proteins
3. DIABLO promotes apoptosis by removing MIHA/XIAP from processed caspase 9
4. Inhibitor of apoptosis proteins and their relatives: IAPs and other BIRPs
5. Structural and biochemical basis of apoptotic activation by Smac/DIABLO
6. Molecular determinants of the caspase-promoting activity of Smac/DIABLO and its role in the death receptor pathway
7. Genetic control of programmed cell death in Drosophila
8. The head involution defective gene of drosophila melanogaster functions in programmed cell death
9. Grim, a novel cell death gene in drosophila
10. Cell killing by the drosophila gene reaper
11. Inhibition of reaper-induced apoptosis by interaction with inhibitor of apoptosis proteins (iaps)
12. Inhibitor of apoptosis proteins physically interact with and block apoptosis induced by drosophila proteins hid and grim
13. The Drosophila caspase inhibitor DIAP1 is essential for cell survival and is negatively regulated by HID
14. Structural basis of IAP recognition by Smac/DIABLO
15. Structural basis for binding of Smac/DIABLO to the XIAP BIR3 domain
16. Sequence as well as functional similarity for DIABLO/Smac and Grim, Reaper and Hid?
17. Structural analysis of a functional diap1 fragment bound to grim and hid peptides
18. A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis
19. Structural basis for the inhibition of caspase-3 by XIAP
20. Structural basis of caspase inhibition by XIAP: Differential roles of the linker versus the BIR domain
21. Structural basis of caspase-7 inhibition by XIAP
22. Direct inhibition of caspase 3 is dispensable for the anti-apoptotic activity of XIAP
23. The inhibitot of apoptosis protein-binding domain of Smac is not essential for its proapoptotic activity
24. Reaper-induced dissociation of a Scythe-sequestered cytochrome c-releasing activity
25. Identification of XAF1 as an antagonist of XIAP anti-Caspase activity