loading...| Preferred Name | Caspase-8 processing | |
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Reviewed: Fitzgerald, Katherine A, 2012-11-13 Authored: Shamovsky, V, 2012-05-15 TLR3/4 signaling component were shown to mediate apoptosis in various human cell lines in the FADD:caspasse-8-dependent manner [Kalai M et al 2002; Kaiser WJ and Offermann MK 2005; Estornes Y et al 2012]. Caspase-8 zymogens (procaspase-8) are present in the cells as inactive monomers, containing a large N-terminal prodomain with two death effector domains (DED), and a C-terminal catalytic subunit composed of small and a large domains separated by a smaller linker region [Donepudi M et al 2003; Keller N et al 2009]. Dimerization is required for caspase-8 activation [Donepudi M et al 2003]. The dimerization event occurs at the receptor signaling complex. Once dimerized, caspase-8 zymogen undergoes a series of autoproteolytic cleavage events at aspartic acid residues in their interdomain linker regions. A second cleavage event between the the N-terminal prodomain and the catalytic domain releases the active caspase from the activation complex into the cytosol. The resulting fully active enzyme is a homodimer of catalytic domains, where each domain is compsed of a large p18 and a small p10 subunit [Keller N et al 2009; Oberst A et al 2010]. Edited: Shamovsky, V, 2012-11-19 |
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http://purl.obolibrary.org/obo/HINO_0009311 |
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| comment |
Reviewed: Fitzgerald, Katherine A, 2012-11-13 Authored: Shamovsky, V, 2012-05-15 TLR3/4 signaling component were shown to mediate apoptosis in various human cell lines in the FADD:caspasse-8-dependent manner [Kalai M et al 2002; Kaiser WJ and Offermann MK 2005; Estornes Y et al 2012]. Caspase-8 zymogens (procaspase-8) are present in the cells as inactive monomers, containing a large N-terminal prodomain with two death effector domains (DED), and a C-terminal catalytic subunit composed of small and a large domains separated by a smaller linker region [Donepudi M et al 2003; Keller N et al 2009]. Dimerization is required for caspase-8 activation [Donepudi M et al 2003]. The dimerization event occurs at the receptor signaling complex. Once dimerized, caspase-8 zymogen undergoes a series of autoproteolytic cleavage events at aspartic acid residues in their interdomain linker regions. A second cleavage event between the the N-terminal prodomain and the catalytic domain releases the active caspase from the activation complex into the cytosol. The resulting fully active enzyme is a homodimer of catalytic domains, where each domain is compsed of a large p18 and a small p10 subunit [Keller N et al 2009; Oberst A et al 2010]. Edited: Shamovsky, V, 2012-11-19 |
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| definition source |
Pubmed12181749 Pubmed12620240 Pubmed20308068 Reactome, http://www.reactome.org Pubmed15814722 Pubmed19278658 Pubmed22421964 Pubmed21737330 |
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Caspase-8 processing |
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| prefixIRI |
HINO:0009311 |
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| prefLabel |
Caspase-8 processing |
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| seeAlso |
ReactomeREACT_150381 Reactome Database ID Release 432562564 EC Number: 3.4.22 GENE ONTOLOGYGO:0008624 |
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