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We began analyzing https://journals.biologists.com/jcs/article/117/21/5035/28059/Mechanism-of-Dronc-activation-in-Drosophila-cells, but it redirected us to https://journals.biologists.com/jcs/article/117/21/5035/28059/Mechanism-of-Dronc-activation-in-Drosophila-cells. The analysis below is for the second page.

Title[redir]:
Mechanism of Dronc activation in Drosophila cells | Journal of Cell Science | The Company of Biologists
Description:
Proteolytic processing is required for the activation of most caspases. However, recent reports have suggested that the activation of the mammalian initiator caspase caspase-9 occurs during dimerization rather than after processing. Previously, we reported that, in normal living Drosophila S2 cells, the initiator caspase Dronc is continuously processed to a 40 kDa form we called Pr1 and that, during apoptosis, a second processed form of 37 kDa is also observed, which we called Pr2. In this study, we determined that Dronc Pr1 is the result of Dronc autoprocessing at amino acid E352, whereas Pr2 results from Drice cleaving full-length Dronc at amino acid D135. By using purified recombinant proteins and expressing Dronc cleavage mutants in S2 cells, we determined that autoprocessing at E352 is crucial for Dronc caspase activity, whereas Drice cleavage at D135 has little effect on Dronc activity. Suppression of the oligomerizing factor Dark by RNA interference revealed that Dark is required for Dronc autoprocessing at E352, whereas RNA interference of the effector caspase Drice revealed that Drice is also required for apoptosis in S2 cells. These results provide the first details of the mechanisms regulating initiator caspase activation in an invertebrate organism.

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open menu article research article cell science journal fast-tracked decision making jcs fast-track option dronc caspase activity initiator caspase dronc journals journal search purchase israel muro purified recombinant proteins google scholar crossref cambridge cb24 9lf �cell biology cell biology rna interference revealed guest editors ana amino acid d135 prokaryotic intracytoplasmic membranes company limited article information amino acid e352 oligomerizing factor dark dronc activity skip view access $30 processing drice cleavage institution sign permissions sign rights reserved company drosophila cells s2 cells special issue cell sci manuscripts full set content rna interference drosophila melanogaster register dronc activation colleagues provide decision letters initial decision dronc pr1 account jcs editors manuscript

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            affiliation:Molecular, Cellular, and Developmental Biology Program, Division of Biology, Ackert Hall, Kansas State University, Manhattan, KS 66506, USA
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            affiliation:Molecular, Cellular, and Developmental Biology Program, Division of Biology, Ackert Hall, Kansas State University, Manhattan, KS 66506, USA
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            affiliation:Molecular, Cellular, and Developmental Biology Program, Division of Biology, Ackert Hall, Kansas State University, Manhattan, KS 66506, USA
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      description:Proteolytic processing is required for the activation of most caspases. However, recent reports have suggested that the activation of the mammalian initiator caspase caspase-9 occurs during dimerization rather than after processing. Previously, we reported that, in normal living Drosophila S2 cells, the initiator caspase Dronc is continuously processed to a 40 kDa form we called Pr1 and that, during apoptosis, a second processed form of 37 kDa is also observed, which we called Pr2. In this study, we determined that Dronc Pr1 is the result of Dronc autoprocessing at amino acid E352, whereas Pr2 results from Drice cleaving full-length Dronc at amino acid D135. By using purified recombinant proteins and expressing Dronc cleavage mutants in S2 cells, we determined that autoprocessing at E352 is crucial for Dronc caspase activity, whereas Drice cleavage at D135 has little effect on Dronc activity. Suppression of the oligomerizing factor Dark by RNA interference revealed that Dark is required for Dronc autoprocessing at E352, whereas RNA interference of the effector caspase Drice revealed that Drice is also required for apoptosis in S2 cells. These results provide the first details of the mechanisms regulating initiator caspase activation in an invertebrate organism.
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      headline:Mechanism of Dronc activation in Drosophila cells
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      affiliation:Molecular, Cellular, and Developmental Biology Program, Division of Biology, Ackert Hall, Kansas State University, Manhattan, KS 66506, USA
      name:Clem, Rollie J.
      affiliation:Molecular, Cellular, and Developmental Biology Program, Division of Biology, Ackert Hall, Kansas State University, Manhattan, KS 66506, USA

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