ArticleThe EMBO journal1997
drICE is an essential caspase required for apoptotic activity in Drosophila cells.
Article in The EMBO journal, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 47 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
47 citing papers in PubMed, 146 citations in OpenAlex.
- Histone acetylation homeodynamics navigates cell survival and apoptosis.Nature communications · 2025Article
- The mechanism underlying toxicity of a venom peptide against insects reveals how ants are master at disrupting membranes.iScience · 2023Article
- Drosophila caspases as guardians of host-microbe interactions.Cell death and differentiation · 2023Review
- JNK is antagonized to ensure the correct number of interommatidial cells pattern the Drosophila retina.Developmental biology · 2018Article
- Article
- Drosophila caspase activity is required independently of apoptosis to produce active TNF/Eiger during nociceptive sensitization.Cell death & disease · 2017Article
- Programmed cell death acts at different stages of Drosophila neurodevelopment to shape the central nervous system.FEBS letters · 2016Review
- Nanos-mediated repression of hid protects larval sensory neurons after a global switch in sensitivity to apoptotic signals.Development (Cambridge, England) · 2016Article
- Article
- The Human Bcl-2 Family Member Bcl-rambo Localizes to Mitochondria and Induces Apoptosis and Morphological Aberrations in Drosophila.PloS one · 2016Article
- The function of Drosophila p53 isoforms in apoptosis.Cell death and differentiation · 2015Article
- Essential versus accessory aspects of cell death: recommendations of the NCCD 2015.Cell death and differentiation · 2015Review
- Genetic models of apoptosis-induced proliferation decipher activation of JNK and identify a requirement of EGFR signaling for tissue regenerative responses in Drosophila.PLoS genetics · 2014Article
- Caspases: a molecular switch node in the crosstalk between autophagy and apoptosis.International journal of biological sciences · 2014Review
- Caspase-dependent regulation of the ubiquitin-proteasome system through direct substrate targeting.Proceedings of the National Academy of Sciences of the United States of America · 2013Article
- A comprehensive characterization of the caspase gene family in insects from the order Lepidoptera.BMC genomics · 2011Article
- Identification and expression of caspase-1 gene under heat stress in insecticide-susceptible and -resistant Plutella xylostella (Lepidoptera: Plutellidae).Molecular biology reports · 2011Article
- Apoptosis, stem cells, and tissue regeneration.Science signaling · 2010Review
- A caspase-like decoy molecule enhances the activity of a paralogous caspase in the yellow fever mosquito, Aedes aegypti.Insect biochemistry and molecular biology · 2010Article
- Non-caspase proteases: triggers or amplifiers of apoptosis?Cellular and molecular life sciences : CMLS · 2010Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Caspases are involved in the execution of cell death in all multicellular organisms so far studied, including the nematode worm, fruit fly and vertebrates. While Caenorhabditis elegans has only a single identified caspase, CED-3, whose activity is absolutely required for all developmental programmed cell deaths, most mammalian cell types express multiple caspases with varying specificities. The fruit fly Drosophila melanogaster is genetically tractable, less complex than vertebrates and possesses two known caspases, DCP-1 and drICE. The fly may therefore provide a good model system for examining the hierarchy and relative roles of individual caspases in the execution of apoptosis. We have examined the role of drICE in in vitro apoptosis of the D.melanogaster cell line S2. We show that cytoplasmic lysates made from S2 cells undergoing apoptosis induced by either reaper (rpr) expression or cycloheximide treatment contain a caspase activity with DEVD specificity which can cleave p35, lamin DmO, drICE and DCP-1 in vitro, and which can trigger chromatin condensation in isolated nuclei. Using antibodies specific to drICE, we show that immunodepletion of drICE from these lysates is sufficient to remove most measurable in vitro apoptotic activity, and that re-addition of exogenous drICE to such immunodepleted lysates restores apoptotic activity. We conclude that, at least in S2 cells, drICE can be the sole caspase effector of apoptosis.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.