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TitleStructural insights into CED-3 activation.
Journal, issue, pagesLife Sci Alliance, Vol. 6, Issue 9, Year 2023
Publish dateJul 4, 2023
AuthorsYini Li / Lu Tian / Ying Zhang / Yigong Shi /
PubMed AbstractIn , onset of programmed cell death is marked with the activation of CED-3, a process that requires assembly of the CED-4 apoptosome. Activated CED-3 forms a holoenzyme with the CED-4 apoptosome to ...In , onset of programmed cell death is marked with the activation of CED-3, a process that requires assembly of the CED-4 apoptosome. Activated CED-3 forms a holoenzyme with the CED-4 apoptosome to cleave a wide range of substrates, leading to irreversible cell death. Despite decades of investigations, the underlying mechanism of CED-4-facilitated CED-3 activation remains elusive. Here, we report cryo-EM structures of the CED-4 apoptosome and three distinct CED-4/CED-3 complexes that mimic different activation stages for CED-3. In addition to the previously reported octamer in crystal structures, CED-4, alone or in complex with CED-3, exists in multiple oligomeric states. Supported by biochemical analyses, we show that the conserved CARD-CARD interaction promotes CED-3 activation, and initiation of programmed cell death is regulated by the dynamic organization of the CED-4 apoptosome.
External linksLife Sci Alliance / PubMed:37402593 / PubMed Central
MethodsEM (single particle)
Resolution3.0 - 4.2 Å
Structure data

36450

8jns

EMDB-36450, PDB-8jns:
cryo-EM structure of a CED-4 hexamer
Method: EM (single particle) / Resolution: 4.2 Å

36451

8jo0

EMDB-36451, PDB-8jo0:
The Cryo-EM structure of a heptameric CED-4/CED-3 catalytic complex
Method: EM (single particle) / Resolution: 3.6 Å

36459

8jol

EMDB-36459, PDB-8jol:
cryo-EM structure of the CED-4/CED-3 holoenzyme
Method: EM (single particle) / Resolution: 3.0 Å

Chemicals

ChemComp-MG:
Unknown entry

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

Source
  • caenorhabditis elegans (invertebrata)
KeywordsAPOPTOSIS / CED-4 apoptosome / Hexamer / CED-4 / CED-3 catalytic domain / CED-3 / holoenzyme

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