Activating Compound | Comment | Organism | Structure |
---|---|---|---|
Fas death domain | FADD, activating caspase-8 via its death-effector domain, DED. FADD dimerizes on binding to Fas, a crucial event that greatly enhances both the FADD-Fas interaction and caspase-8 activation | Homo sapiens | |
additional information | caspase-8 is activated by homodimerization, which also leads to autoproteolytic processing of the enzyme into multiple smaller species | Homo sapiens |
Protein Variants | Comment | Organism |
---|---|---|
C360S | a caspase-8 inactive mutant, shows no LRRK2-induced neuronal death, knockdown of caspase-8 by siRNA blocks LRRK2-induced neurotoxicity and neurodegeneration | Homo sapiens |
Localization | Comment | Organism | GeneOntology No. | Textmining |
---|---|---|---|---|
additional information | LRRK2, FADD, and caspase-8 are components of a multiprotein complex | Homo sapiens | - |
- |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | Homo sapiens | LRRK2-induced neuronal death is caspase-8-dependent. Fas death domain, FADD, recruits caspase-8 to LRRK2. FADD transduces death signals by binding to ligand-activated Fas via its DD and recruiting and activating caspase-8 via its death-effector domain, DED. The Parkinson disease protein leucine-rich repeat kinase 2 transduces death signals via Fas-associated protein with death domain and caspase-8 in a cellular model of neurodegeneration. In primary neuronal culture LRRK2-mediated neurodegeneration is prevented by the functional inhibition of FADD or depletion of caspase-8, two key elements of the extrinsic cell death pathway, overview | ? | - |
? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Homo sapiens | - |
- |
- |
Posttranslational Modification | Comment | Organism |
---|---|---|
proteolytic modification | caspase-8 is activated by homodimerization, which also leads to autoproteolytic processing of the enzyme into multiple smaller species | Homo sapiens |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
brain | healthy and Parkinson disease brains, caspase-8 is selectively activated in brain tissue from patients with LRRK2 Parkinson disease | Homo sapiens | - |
corpus striatum | - |
Homo sapiens | - |
neuron | - |
Homo sapiens | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
additional information | LRRK2-induced neuronal death is caspase-8-dependent. Fas death domain, FADD, recruits caspase-8 to LRRK2. FADD transduces death signals by binding to ligand-activated Fas via its DD and recruiting and activating caspase-8 via its death-effector domain, DED. The Parkinson disease protein leucine-rich repeat kinase 2 transduces death signals via Fas-associated protein with death domain and caspase-8 in a cellular model of neurodegeneration. In primary neuronal culture LRRK2-mediated neurodegeneration is prevented by the functional inhibition of FADD or depletion of caspase-8, two key elements of the extrinsic cell death pathway, overview | Homo sapiens | ? | - |
? |
Subunits | Comment | Organism |
---|---|---|
dimer | caspase-8 is activated by homodimerization, which also leads to autoproteolytic processing of the enzyme into multiple smaller species | Homo sapiens |
More | LRRK2, FADD, and caspase-8 are components of a multiprotein complex | Homo sapiens |
Synonyms | Comment | Organism |
---|---|---|
Casp8 | - |
Homo sapiens |