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Literature summary for 3.4.22.61 extracted from

  • Ho, C.C.; Rideout, H.J.; Ribe, E.; Troy, C.M.; Dauer, W.T.
    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 (2009), J. Neurosci., 29, 1011-1016.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.22.61

Activating Compound

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

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

Localization Comment Organism GeneOntology No. Textmining
additional information LRRK2, FADD, and caspase-8 are components of a multiprotein complex Homo sapiens
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-

Natural Substrates/ Products (Substrates)

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 ?
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 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens
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-
-

Posttranslational Modification

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

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
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corpus striatum
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 Homo sapiens
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neuron
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 Homo sapiens
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Substrates and Products (Substrate)

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 ?
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 ?

Subunits

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

Synonyms Comment Organism
Casp8
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 Homo sapiens