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Literature summary for 3.4.22.61 extracted from

  • Oberst, A.; Green, D.R.
    It cuts both ways: reconciling the dual roles of caspase 8 in cell death and survival (2011), Nat. Rev. Mol. Cell Biol., 12, 757-763.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.61

Inhibitors

Inhibitors Comment Organism Structure
FLIPL protein i.e. FLICE-like inhibitory protein long, inhibits apoptotic caspase 8 activation. FLIP is homologous to caspase 8 but lacks catalytic residues. FLIP forms a heterodimer with caspase 8, which prevents apoptosis induction. Dynamic ubiquitylation is at least partially responsible for controlling the activation of caspase 8 by FLIPL Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
RIPK1 + H2O Homo sapiens Lys63-linked RIPK1 ubiquitylation is required to render RIPK1 susceptible to caspase 8-mediated cleavage, the mechanism by which RIPK1 signalling is suppressed in this context ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification caspase proenzymes are induced to dimerize, and this dimerization leads to enzyme activation, mechanism of caspase 8 activation, detailed overview. In the case of caspase 8, dimerization is followed by interdomain cleavage events, first between the large and small subunits and subsequently between the large subunit and the prodomain. These cleavage events stabilize the caspase 8 homodimer and remove the prodomain, leading to formation of a fully active enzyme composed of two large and two small subunits Homo sapiens
side-chain modification both degradative and non-degradative ubiquitylation have central roles in the control of nuclear factor-kappaB activation, as well as caspase 8 and receptor-interacting protein kinase 1, RIPK1, signalling, overview. Caspase 8 is modified by non-degradative ubiquitin chains allowing the activation of a non-cleavable caspase 8 mutant. Dynamic ubiquitylation is at least partially responsible for controlling the activation of caspase 8 by FLICE-like inhibitory protein long, FLIPL Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
T-lymphocyte
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 Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
RIPK1 + H2O
-
 Homo sapiens ?
-
 ?
RIPK1 + H2O Lys63-linked RIPK1 ubiquitylation is required to render RIPK1 susceptible to caspase 8-mediated cleavage, the mechanism by which RIPK1 signalling is suppressed in this context Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
dimer caspase proenzymes are induced to dimerize, and this dimerization leads to enzyme activation. In the case of caspase 8, dimerization is followed by interdomain cleavage events, first between the large and small subunits and subsequently between the large subunit and the prodomain. These cleavage events stabilize the caspase 8 homodimer and remove the prodomain, leading to formation of a fully active enzyme composed of two large and two small subunits Homo sapiens

Synonyms

Synonyms Comment Organism
caspase 8
-
 Homo sapiens

General Information

General Information Comment Organism
malfunction proliferative defects of caspase 8-deficient T cells and B cells. Caspase-8 deficiency causes programmed necrotic cell death Homo sapiens
metabolism recruitment of caspase 8 and FLIP to a RIPK1-containing complex determines cell fate, overview Homo sapiens
physiological function caspase 8 can initiate apoptosis in response to cell surface receptor activation, but it is also required for embryonic development and immune cell proliferation, defined by suppression of receptor-interacting protein kinase 3, a kinase that triggers an alternative form of cell death called programmed necrosis. The extrinsic apoptosis, is mediated by a group of receptors of the tumour necrosis factor, TNF, superfamily called the death receptors. Caspase 8 is further implicated in cell motility, metastasis, and suppression of inflammation. The non-apoptotic roles of FADD and caspase 8 are involved the sup­pression of RIPK3-dependent programmed necrosis, the caspase 8–FLIP heterodimer is implicated in carrying out the suppression of RIPK3 signalling. Mechanism of caspase 8 activation, detailed overview Homo sapiens