ArticleThe Journal of cell biology2002
A novel Apaf-1-independent putative caspase-2 activation complex.
Article in The Journal of cell biology, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 55 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
55 citing papers in PubMed, 162 citations in OpenAlex.
- Caspase-2 is a condensate-mediated deubiquitinase in protein quality control.Nature cell biology · 2024Article
- Gene Expression Regulation and the Signal Transduction of Programmed Cell Death.Current issues in molecular biology · 2024Review
- Traditional Chinese medicine for colorectal cancer treatment: potential targets and mechanisms of action.Chinese medicine · 2023Review
- Caspase-2 is a mediator of apoptotic signaling in response to gemtuzumab ozogamicin in acute myeloid leukemia.Cell death discovery · 2022Article
- The p53-caspase-2 axis in the cell cycle and DNA damage response.Experimental & molecular medicine · 2021Review
- Phosphorylation by Aurora B kinase regulates caspase-2 activity and function.Cell death and differentiation · 2021Article
- The Role of Caspase-2 in Regulating Cell Fate.Cells · 2020Review
- Mechanistic Interplay Between Autophagy and Apoptotic Signaling in Endosulfan-Induced Dopaminergic Neurotoxicity: Relevance to the Adverse Outcome Pathway in Pesticide Neurotoxicity.Toxicological sciences : an official journal of the Society of Toxicology · 2019Article
- Necroptosis andFrontiers in microbiology · 2019Article
- New insights into apoptosome structure and function.Cell death and differentiation · 2018Review
- Mitotic Catastrophe in BC3H1 Cells following Yessotoxin Exposure.Frontiers in cell and developmental biology · 2017Article
- MiR-125a-5p decreases after long non-coding RNA HOTAIR knockdown to promote cancer cell apoptosis by releasing caspase 2.Cell death & disease · 2016Article
- Cellular mechanisms controlling caspase activation and function.Cold Spring Harbor perspectives in biology · 2013Review
- Review
- Role for caspase-2 during pore-forming toxin-mediated apoptosis.Cell cycle (Georgetown, Tex.) · 2012Article
- PIDD death-domain phosphorylation by ATM controls prodeath versus prosurvival PIDDosome signaling.Molecular cell · 2012Article
- Chemosensitivity is controlled by p63 modification with ubiquitin-like protein ISG15.The Journal of clinical investigation · 2012Article
- Caspase-2 is an initiator caspase responsible for pore-forming toxin-mediated apoptosis.The EMBO journal · 2012Article
- Cutting edge: the "death" adaptor CRADD/RAIDD targets BCL10 and suppresses agonist-induced cytokine expression in T lymphocytes.Journal of immunology (Baltimore, Md. : 1950) · 2012Article
- The PIDDosome, DNA-damage-induced apoptosis and beyond.Cell death and differentiation · 2012Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Caspase activation is a key event in apoptosis execution. In stress-induced apoptosis, the mitochondrial pathway of caspase activation is believed to be of central importance. In this pathway, cytochrome c released from mitochondria facilitates the formation of an Apaf-1 apoptosome that recruits and activates caspase-9. Recent data indicate that in some cells caspase-9 may not be the initiator caspase in stress-mediated apoptosis because caspase-2 is required upstream of mitochondria for the release of cytochrome c and other apoptogenic factors. To determine how caspase-2 is activated, we have studied the formation of a complex that mediates caspase-2 activation. Using gel filtration analysis of cell lysates, we show that caspase-2 is spontaneously recruited to a large protein complex independent of cytochrome c and Apaf-1 and that recruitment of caspase-2 to this complex is sufficient to mediate its activation. Using substrate-binding assays, we also provide the first evidence that caspase-2 activation may occur without processing of the precursor molecule. Our data are consistent with a model where caspase-2 activation occurs by oligomerization, independent of the Apaf-1 apoptosome.
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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.