Ubiquitin-protein ligase activity of X-linked inhibitor of apoptosis protein promotes proteasomal degradation of caspase-3 and enhances its anti-apoptotic effect in Fas-induced cell death
By Yasuyuki Suzuki, Yui Nakabayashi, R. Takahashi. Proceedings of the National Academy of Sciences of the United States of America, 2001
688 citations recorded by the source corpus.
Subfields: Epidemiology, Molecular Biology
View Paper: https://www.semanticscholar.org/paper/a619b0b0d8b6c0f64a8d262f6a6fbe74e56d584c
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Citations in the corpus
- HECT and RING finger families of E3 ubiquitin ligases at a glance (2012, background): “Xchromosome-linked IAP (XIAP) binds to caspases 3, 7 and 9, directly blocks their catalytic activity and, additionally, regulates their protein levels through ubiquitylation and subsequent degradation (Morizane et al., 2005; Schile et al., 2008; Suzuki et al., 2001).”
- Mechanisms of caspase activation and inhibition during apoptosis. (2002, background): “This function is countered by the proapoptotic proteins, independent groups (Hedge et al., 2002; Martin et al., 2002; Suzuki et al., 2001a; van Loo et al., 2002; VerhagenReaper, Grim, Hid, and more recently, Sickle (Christich et al., 2002; Srinivasula et al., 2002; Wing et al., 2002), et al., 2002).”
- Human inhibitor of apoptosis proteins: why XIAP is the black sheep of the family (2006, background): “Moreover, XIAP-directed caspase ubiquitination might not result in degradation by the proteasome (Creagh et al, 2004; Hao et al, 2004; Morizane et al, 2005; Suzuki et al, 2001).”
- The expanding role of mitochondria in apoptosis. (2001, background): “The inhibition could become permanent because many IAPs also contain a RING finger domain that may target the bound caspases for proteasome degradation (Yang et al. 2000; Suzuki et al. 2001).”
- IAP proteins: blocking the road to death's door (2002, background): “The RING domains of XIAP, c-IAP1 and c-IAP2 show E3 activit”
- Cellular mechanisms controlling caspase activation and function. (2013, background): “Other work has shown that XIAP can polyubiquitylate active caspase-3 (not procaspase-3), leading to its proteasome-dependent degradation (Suzuki et al. 2001).”