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TitleThe holo-apoptosome: activation of procaspase-9 and interactions with caspase-3.
Journal, issue, pagesStructure, Vol. 19, Issue 8, Page 1084-1096, Year 2011
Publish dateAug 10, 2011
AuthorsShujun Yuan / Xinchao Yu / John M Asara / John E Heuser / Steven J Ludtke / Christopher W Akey /
PubMed AbstractActivation of procaspase-9 on the apoptosome is a pivotal step in the intrinsic cell death pathway. We now provide further evidence that caspase recruitment domains of pc-9 and Apaf-1 form a CARD- ...Activation of procaspase-9 on the apoptosome is a pivotal step in the intrinsic cell death pathway. We now provide further evidence that caspase recruitment domains of pc-9 and Apaf-1 form a CARD-CARD disk that is flexibly tethered to the apoptosome. In addition, a 3D reconstruction of the pc-9 apoptosome was calculated without symmetry restraints. In this structure, p20 and p10 catalytic domains of a single pc-9 interact with nucleotide binding domains of adjacent Apaf-1 subunits. Together, disk assembly and pc-9 binding create an asymmetric proteolysis machine. We also show that CARD-p20 and p20-p10 linkers play important roles in pc-9 activation. Based on the data, we propose a proximity-induced association model for pc-9 activation on the apoptosome. We also show that pc-9 and caspase-3 have overlapping binding sites on the central hub. These binding sites may play a role in pc-3 activation and could allow the formation of hybrid apoptosomes with pc-9 and caspase-3 proteolytic activities.
External linksStructure / PubMed:21827945 / PubMed Central
MethodsEM (single particle)
Resolution16.9 Å
Structure data

EMDB-1931:
Map of the apoptosome-procaspase-9 complex
Method: EM (single particle) / Resolution: 16.9 Å

Source
  • Homo sapiens (human)
  • Bos taurus (cattle)

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