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Cryo-EM structural analysis of FADD: Caspase-8 complexes defines the catalytic dimer architecture for co-ordinated control of cell fate

ABSTRACT: Uncovering the molecular architecture of the core FADD:Caspase-8 complex and how this is altered by regulatory partners, such as the cell death inhibitor c-FLIP, is essential to understand co-ordination of cell fate. Here, using electron microscopy, we visualize for the first time fulllength procaspase-8 in a complex with FADD. Our structural analysis reveals how the FADDnucleated tandem death effector domain (tDED) helical filament is required to correctly orientate procaspase-8 catalytic domains, enabling activation via anti-parallel dimerization.

INSTRUMENT(S):

ORGANISM(S): Homo Sapiens (human)

TISSUE(S): Cell Culture, Kidney Cell

SUBMITTER: Rebekah Jukes-Jones

LAB HEAD: Marion M. MacFarlane

PROVIDER: PXD022408 | Pride | 2021-02-08

REPOSITORIES: Pride

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	JF_FADDCasp8_GDG2_fr10_LG_241017001.mzid.gz	Mzid
	JF_FADDCasp8_GDG2_fr10_LG_241017001.mzid_JF_FADDCasp8_GDG2_fr10_LG_241017001.MGF	Mzid
	JF_FADDCasp8_GDG2_fr10_LG_241017001.raw.zip	Raw
	JF_FADDCasp8_GDG2_fr10_LG_241017002.mzid.gz	Mzid
	JF_FADDCasp8_GDG2_fr10_LG_241017002.mzid_JF_FADDCasp8_GDG2_fr10_LG_241017002.MGF	Mzid

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Caspase-8 and FADD prevent spontaneous ZBP1 expression and necroptosis

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