1999
DOI: 10.1038/21124
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Abstract: Caspase-9-mediated apoptosis (programmed cell death) plays a central role in the development and homeostasis of all multicellular organisms. Mature caspase-9 is derived from its procaspase precursor as a result of recruitment by the activating factor Apaf-1. The crystal structures of the caspase-recruitment domain of Apaf-1 by itself and in complex with the prodomain of procaspase-9 have been determined at 1.6 and 2.5 A resolution, respectively. These structures and other evidence reveal that each molecule of … Show more

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Cited by 405 publications
(434 citation statements)
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“…In a similar context, it was shown that caspase-8 forms a complex with Apaf-1 (Hu et al, 1998), which implies that anticancer drugs activate caspase-8 downstream of mitochondrial damage. Supportive for an interaction of Apaf-1 with caspase-8 might be the solution structure of the Apaf-1 CARD domain, which is structurally related to the DED of FADD (Qin et al, 1999;Day et al, 1999). To investigate whether caspase-8 could function as an initiator caspase in the mitochondrial pathway, we used caspase-8-de®-cient Jurkat cells.…”
Section: Discussionmentioning
confidence: 99%
See 1 more Smart Citation
“…In a similar context, it was shown that caspase-8 forms a complex with Apaf-1 (Hu et al, 1998), which implies that anticancer drugs activate caspase-8 downstream of mitochondrial damage. Supportive for an interaction of Apaf-1 with caspase-8 might be the solution structure of the Apaf-1 CARD domain, which is structurally related to the DED of FADD (Qin et al, 1999;Day et al, 1999). To investigate whether caspase-8 could function as an initiator caspase in the mitochondrial pathway, we used caspase-8-de®-cient Jurkat cells.…”
Section: Discussionmentioning
confidence: 99%
“…Most interestingly, caspase-8 was also activated by anticancer drugs in the absence of death receptor signaling Wesselborg et al, 1999), although it remains unclear whether death receptorindependent activation of caspase-8 is physiologically relevant. Since the DED of FADD has structural resemblance with the CARD motif (Qin et al, 1999;Day et al, 1999), it may be speculated that caspase-8 could be recruited to Apaf-1, in a similar fashion as caspase-9. In fact, it has been demonstrated that caspase-8 can interact with Apaf-1 or its homolog Ced-4 (Chinnaiyan et al, 1997; Hu et al, 1998), and that in some instances caspase-8 is necessary for Ced-4 mediated cell death (Han et al, 1998).…”
Section: Introductionmentioning
confidence: 99%
“…Afterward, pro-caspase-9 is activated via reciprocal cleavage, and by this way, apoptosome complex also become activated. Then, caspase-3 is cleaved and activated via caspase-9 found in the active apoptosome complex [60].…”
Section: Caspase Family Membersmentioning
confidence: 99%
“…Cytochrome c can bind to a cytosolic protein called Apaf-1, and in turn, this complex binds to pro-caspase 9 by interacting with the caspase recruitment domain (CARD), resulting in the formation of the apoptosome and transactivation of caspase 9 (Li et al, 1997;Cain et al, 2002). The activated caspase 9 can then initiate the caspase cascade by activation of downstream caspase 3, -6, and -7 (Budihardjo et al, 1999), ultimately leading to cell death (Li et al, 1997;Qin et al, 1999).…”
Section: Introductionmentioning
confidence: 99%