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Literature summary for 3.4.22.56 extracted from

  • Edelmann, B.; Bertsch, U.; Tchikov, V.; Winoto-Morbach, S.; Perrotta, C.; Jakob, M.; Adam-Klages, S.; Kabelitz, D.; Schuetze, S.
    Caspase-8 and caspase-7 sequentially mediate proteolytic activation of acid sphingomyelinase in TNF-R1 receptosomes (2011), EMBO J., 30, 379-394.
    View publication on PubMedView publication on EuropePMC
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Localization

Localization Comment Organism GeneOntology No. Textmining
additional information caspase-3 and its activation is not associated with TNF receptosomes. Neither caspase-3 nor cleaved caspase-3 are present in receptosomes Homo sapiens
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Organism

Organism UniProt Comment Textmining
Homo sapiens
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Posttranslational Modification

Posttranslational Modification Comment Organism
proteolytic modification cleavage of procaspase-3 to the active 17 kDa form. Caspase-3 activation occurs after TNF stimulation at later time points and is not associated with TNF receptosomes Homo sapiens

Source Tissue

Source Tissue Comment Organism Textmining
HeLa cell
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 Homo sapiens
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JURKAT cell
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 Homo sapiens
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General Information

General Information Comment Organism
metabolism tumour necrosis factor, TNF, induced ceramide production by endosomal acid sphingomyelinase, A-SMase, couples to apoptosis signalling via activation of cathepsin D and cleavage of Bid, resulting in caspase-9 and caspase-3 activation Homo sapiens
additional information active caspase-3 does not colocalize with internalized TNF-R1 receptosomes Homo sapiens
physiological function caspase-3 activates acid sphingomyelinase, i.e. A-SMase, but pro-A-SMase is not a direct substrate for caspase-3 Homo sapiens