A conserved XIAP-interaction motif in caspase-9 and Smac/DIABLO regulates caspase activity and apoptosis

By S. Srinivasula, R. Hegde, Ayman Saleh, P. Datta, E. Shiozaki, J. Chai, R. Lee, P. Robbins, T. Fernandes-Alnemri, Yigong Shi and 1 more. Nature, 2001

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Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/19425b81b29f53cb899a928dcbeddc448c1f828f

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Citations in the corpus

cIAP1 and cIAP2 facilitate cancer cell survival by functioning as E3 ligases that promote RIP1 ubiquitination. (2008, background): “Once in the cytosol, Smac binds to a groove in the XIAP BIR3 domain that is required for the XIAP-caspase-9 interaction and causes caspase-9 to be released from XIAP inhibition (Srinivasula et al., 2001).”
A unified model for apical caspase activation. (2003, methodology): “After evaporation, the wells were brought to a final concencaspase-9 constructs contained Ala substitutions at residues 306, tration of 10 mM in DMSO based on the resin loading and stored 315, and 330 to prevent autolytic cleavage (Srinivasula et al., 2001) at –20 C.”
Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy (2006, background): “One Smac/DIABLO dimer binds one XIAP molecule by both IAP-binding motifs, one interacting with BIR2 and the other one with BIR3 (Huang et al., 2003).”
Mechanism of XIAP-mediated inhibition of caspase-9. (2003, methodology): “This characteristic loop, with a previouslydicted interaction between the N terminus of the cas- pase-9 small subunit and a highly conserved surface undefined function, is found to play an important role in binding to the BIR3 domain of XIAP.groove on BIR3 (Srinivasula et al., 2001).”
Mechanisms of caspase activation. (2003, background): “As with caspase-8, not only is cleavage unnecessary for activation of caspase-9, but also it is insufficient to produce an active enzyme [3,23].”
Cellular mechanisms controlling caspase activation and function. (2013, background): “XIAP can inhibit caspase-3 and caspase-7 by binding to the active site, and caspase-9 by preventing or reversing dimerization (Deveraux et al. 1997; Chai et al. 2001; Riedl et al. 2001; Srinivasula et al. 2001; Shiozaki et al. 2003).”
Mechanisms of caspase activation and inhibition during apoptosis. (2002, background): “These freshly exposed N-terminal residues play an indispensable role in Smac function; a seven residueBIR3 (Srinivasula et al., 2001).”
Essential versus accessory aspects of cell death: recommendations of the NCCD 2015 (2014, background): “Whether the apoptotic response to extracellular cues requires MOMP or not reportedly depends on the expression levels of X-linked inhibitor of apoptosis (XIAP),(158,159) an ubiquitin ligase with multipronged cytoprotective functions.(160,161) High amounts of XIAP prevent indeed the direct activation”
Role of Bcl-2 family proteins and caspases in the regulation of apoptosis (2011, background): “such as XIAP, c-IAP1, and c-IAP2, bind caspase-3, caspase7, and caspase-9, thereby inhibiting their activation and preventing apoptosis (Table 1) [156, 158–160].”
The role of mitochondrial factors in apoptosis: a Russian roulette with more than one bullet (2002, background): “Omi/HtrA2 interacts with both the BIR2 and BIR3 domains of XIAP, although with higher affinity for the BIR2, as opposed to Smac/DIABLO, which preferentially binds the BIR3 domain.17,20 This selectivity suggests that Omi/HtrA2 may promote preferentially caspase-3 activation rather than caspase-9 acti”