Three-dimensional Structure of a Double Apoptosome Formed by the Drosophila Apaf-1 Related Killer

Yu, Xianjun; Wang, Lai; Acehan, Devrim; Wang, Xiaodong; Akey, Christopher W.

doi:10.1016/j.jmb.2005.10.040

Cited by 116 publications

(157 citation statements)

References 53 publications

(89 reference statements)

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“…42,[63][64][65][66] ARK can assemble into a large apoptosome complex in the presence of dATP. 67 However, cytochrome c is not required for the apoptosome assembly and fails to bind the complex. 67 The 3D structure of the ARK complex at 18.8 A resolution using electron cryo-microscopy showed that eight ARK molecules assemble into an apoptosome-like particle.…”

Section: Activation Of Fly Caspasesmentioning

confidence: 99%

“…67 However, cytochrome c is not required for the apoptosome assembly and fails to bind the complex. 67 The 3D structure of the ARK complex at 18.8 A resolution using electron cryo-microscopy showed that eight ARK molecules assemble into an apoptosome-like particle. 67 Interestingly, the ARK apoptosome is a double-ringed structure.…”

Section: Activation Of Fly Caspasesmentioning

confidence: 99%

“…67 The 3D structure of the ARK complex at 18.8 A resolution using electron cryo-microscopy showed that eight ARK molecules assemble into an apoptosome-like particle. 67 Interestingly, the ARK apoptosome is a double-ringed structure. 67 Currently, the mechanism by which DRONC is recruited and activated by this apoptosome is not understood.…”

Section: Activation Of Fly Caspasesmentioning

confidence: 99%

“…67 Interestingly, the ARK apoptosome is a double-ringed structure. 67 Currently, the mechanism by which DRONC is recruited and activated by this apoptosome is not understood.…”

Section: Activation Of Fly Caspasesmentioning

confidence: 99%

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Caspase function in programmed cell death

2006

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The first proapoptotic caspase, CED-3, was cloned from Caenorhabditis elegans in 1993 and shown to be essential for the developmental death of all somatic cells. Following the discovery of CED-3, caspases have been cloned from several vertebrate and invertebrate species. As reviewed in other articles in this issue of Cell Death and Differentiation, many caspases function in nonapoptotic pathways. However, as is clear from the worm studies, the evolutionarily conserved role of caspases is to execute programmed cell death. In this article, I will specifically focus on caspases that function primarily in cell death execution. In particular, the physiological function of caspases in apoptosis is discussed using examples from the worm, fly and mammals.

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Section: Activation Of Fly Caspasesmentioning

confidence: 99%

Section: Activation Of Fly Caspasesmentioning

confidence: 99%

Section: Activation Of Fly Caspasesmentioning

confidence: 99%

“…67 Interestingly, the ARK apoptosome is a double-ringed structure. 67 Currently, the mechanism by which DRONC is recruited and activated by this apoptosome is not understood.…”

Section: Activation Of Fly Caspasesmentioning

confidence: 99%

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Caspase function in programmed cell death

2006

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“…This is because: (1) no developmental apoptosis defect was observed in mutants of the Drosophila bcl-2 homologs, debcl and buffy [24], 2) apoptosis occurs normally in Drosophila cell lines depleted in Cyt-C [25,26] and 3) structural data showed that the apoptosome can form in the absence of Cyt-c in vitro [27]. Thus, it was suggested that the apoptosome is constitutively active and that the rpr/IAP pathway is sufficient to explain apoptosis in Drosophila.…”

Section: The Role Of Mitochondria In Apoptosismentioning

confidence: 99%

Cell death: what can we learn from flies? Editorial for the special review issue on Drosophila apoptosis

Mollereau

2009

Apoptosis

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The Apoptosome: The Executioner of Mitochondria‐mediated Apoptosis

Ferraro

Cecconi

2009

Encyclopedia of Life Sciences

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The apoptosome is a molecular complex of two major components – the adapter protein apoptotic protease activating factor 1 ( Apaf1 ) and the protease caspase‐9. These are assembled during apoptosis upon Apaf1 interaction with cytochrome c , which is released from the intermembrane space of mitochondria under precise cell death stimuli. Apoptosome assembly triggers effector caspase activation, which – in turn – drives cell demise. Several proteins bind and regulate apoptosome. This complex is found in vertebrates, even though similar functions are played by ortholog proteins through slightly different mechanisms also in lower eukaryotes. Given the involvement of apoptosome dysfunctions in human diseases, this complex is also a relevant molecular target in biomedicine. Key concepts It was a stunning discovery to find out that cytochrome c , essential for adenosine triphosphate (ATP) production and cell life, was involved in a cell death pathway. Apoptosis regulation is essential for avoiding unwanted cell death and allowing the correct development and homoeostasis of the whole organism. Therefore there are several regulators of apoptosome activity. Caspases and Apaf1 have a key phylogenetically conserved role in apoptosis. Apoptosis is evolutionary well‐conserved in terms of its basic mechanisms; however, the role of mitochondria in apoptosis of organisms other than vertebrates needs to be clearly defined.

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Three-dimensional Structure of a Double Apoptosome Formed by the Drosophila Apaf-1 Related Killer

Cited by 116 publications

References 53 publications

Caspase function in programmed cell death

Caspase function in programmed cell death

Cell death: what can we learn from flies? Editorial for the special review issue on Drosophila apoptosis

The Apoptosome: The Executioner of Mitochondria‐mediated Apoptosis

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